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heat shock protein transcriptional repressor HspR
HspR (heat shock protein repressor) binds a widely conserved DNA element known as HAIR (HspR-associated inverted repeat). All members of the seed alignment were found encoded in the vicinity of DnaJ. This HMM represents a strongly conserved central region of about 92 amino acids. Member proteins occur in lineages as distant as Campylobacter, Helicobacter, Mycobacterium, Streptomyces, Bifidobacterium, and Deinococcus. HspR forms a homodimer, although in some species, double-length proteins with a tandem duplication are found (see NF047377). In Mycobacterium tuberculosis, DnaK was shown to bind directly to the HspR-HAIR complex.
ASTN1/2 Fn3 domain
Astrotactin-1 and 2 (ASTN1/2) are integral membrane proteins with a large C-terminal domain, extracellular for ASTN1 and endosome luminal for ASTN-2 [1,2]. They play critical roles in neurodevelopment, and ASTN-2 is also involved in the planar cell polarity pathway in hair cells. This is a domain found in the middle of the C-terminal of ASTN-1 and 2, which comprises a fibronectin type III (Fn(III)) domain [1]. This domain located between the MACPF and annexin domains. The structure of Fn(III) from ASTN2 revealed an unexpected feature which has two additional beta strands folded across the core. The junction between EGF-4 and Fn(III) domains in ASTN2 (but not in ASTN1) is thought to be an inositol triphosphate binding site [1]. Paper describing PDB structure 5j67. [1]. 27249642. Structure of astrotactin-2: a conserved vertebrate-specific and. perforin-like membrane protein involved in neuronal development.. Ni T, Harlos K, Gilbert R;. Open Biol. 2016; [Epub ahead of print]. [2]. 20573900. Astn2, a novel member of the astrotactin gene family, regulates. the trafficking of ASTN1 during glial-guided neuronal migration.. Wilson PM, Fryer RH, Fang Y, Hatten ME;. J Neurosci. 2010;30:8529-8540. (from Pfam)
Kinocilin protein
This family of kinocilin proteins is found in vertebrate. In mouse it has been shown that this protein is expressed primarily in the kinocilium of sensory cells in the inner ear [1]. [1]. 15855039. Initial characterization of kinocilin, a protein of the hair. cell kinocilium.. Leibovici M, Verpy E, Goodyear RJ, Zwaenepoel I, Blanchard S,. Laine S, Richardson GP, Petit C;. Hear Res. 2005;203:144-153. (from Pfam)
BclA C-terminal domain
This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization [1]. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host [2]. [1]. 22405006. Variable lymphocyte receptor recognition of the immunodominant. glycoprotein of Bacillus anthracis spores.. Kirchdoerfer RN, Herrin BR, Han BW, Turnbough CL Jr, Cooper MD,. Wilson IA;. Structure. 2012;20:479-486.. [2]. 17879302. Construction, crystal structure and application of a recombinant. protein that lacks the collagen-like region of BclA from. Bacillus anthracis spores.. Liu CQ, Nuttall SD, Tran H, Wilkins M, Streltsov VA, Alderton. MR;. Biotechnol Bioeng. 2008;99:774-782. (from Pfam)
Sey1 three-helix bundle domain
This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum [1,2,3]. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion [3]. [1]. 9087433. The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily. conserved protein with GTP-binding motifs and is required for. regulated cell enlargement in Arabidopsis.. Wang H, Lockwood SK, Hoeltzel MF, Schiefelbein JW;. Genes Dev 1997;11:799-811.. [2]. 12427979. Function of a plant stress-induced gene, HVA22. Synthetic. enhancement screen with its yeast homolog reveals its role in. vesicular traffic.. Brands A, Ho TH;. Plant Physiol 2002;130:1121-1131.. [3]. 26370501. Structures of the yeast dynamin-like GTPase Sey1p provide. insight into homotypic ER fusion.. Yan L, Sun S, Wang W, Shi J, Hu X, Wang S, Su D, Rao Z, Hu J,. Lou Z;. J Cell Biol. 2015;210:961-972. (from Pfam)
Astrotactin-2 C-terminal beta-hairpin domain
This is a beta-hairpin domain found at the C-terminal region of astrotactin 2 proteins (ASTN-2). ASTN-2 is an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. it consists of multiple polypeptide folds: a perforin-like domain, a minimal epidermal growth factor-like module, a fibronectin type III domain Fn (III) and an annexin-like domain as well as the beta hairpin domain which packs across the fibronectin domain [1]. [1]. 27249642. Structure of astrotactin-2: a conserved vertebrate-specific and. perforin-like membrane protein involved in neuronal development.. Ni T, Harlos K, Gilbert R;. Open Biol. 2016; [Epub ahead of print] (from Pfam)
Otospiralin
This family of proteins, Otospiralin, has a role in maintaining the neurosensory epithelium of the inner ear [1,2]. This family of proteins is found in eukaryotes. Proteins in this family are approximately 90 amino acids in length. [1]. 11880501. Downregulation of otospiralin, a novel inner ear protein, causes. hair cell degeneration and deafness.. Delprat B, Boulanger A, Wang J, Beaudoin V, Guitton MJ, Venteo. S, Dechesne CJ, Pujol R, Lavigne-Rebillard M, Puel JL, Hamel CP;. J Neurosci. 2002;22:1718-1725.. [2]. 18832023. Is otospiralin inner ear specific? Evidence for its expression. in mouse brain.. Decourt B, Hillman D, Bouleau Y, Dulon D, Hafidi A;. Int J Dev Neurosci. 2009;27:87-96. (from Pfam)
Annexin-like domain
This annexin-like domain can be found in astrotactin 2 (Astn-2), an integral membrane perforin-like protein linked to the planar cell polarity pathway in hair cells. The annexin-like domain is closest in fold to repeat three of human annexin V and similarly binds calcium, yet shares no sequence homology with it. Notably, this ASTN-2 annexin-like domain is closer in structure to human annexin repeat 3 than human annexin repeat 3 is to repeat 1. Annexin-like domains are known for their capacity to remodel membranes, triggered by calcium binding, and have also been suggested to be involved in the formation of pores in membranes both are possible biological roles of the ASTN-2 annexin-like domain [1]. [1]. 27249642. Structure of astrotactin-2: a conserved vertebrate-specific and. perforin-like membrane protein involved in neuronal development.. Ni T, Harlos K, Gilbert R;. Open Biol. 2016; [Epub ahead of print] (from Pfam)
MYCBP-associated protein family
This family of eukaryotic proteins includes the mammalian MYCBP-associated proteins. These proteins may be synaptic processes [1] and may have a role in spermatogenesis [2]. [1]. 15607946. Cod106, a novel synaptic protein expressed in sensory hair cells. of the inner ear and in CNS neurons.. Reisinger E, Zimmermann U, Knipper M, Ludwig J, Klocker N,. Fakler B, Oliver D;. Mol Cell Neurosci. 2005;28:106-117.. [2]. 12151104. AMAP-1, a novel testis-specific AMY-1-binding protein, is. differentially expressed during the course of spermatogenesis.. Yukitake H, Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H;. Biochim Biophys Acta. 2002;1577:126-132. (from Pfam)
Protein-arginine deiminase (PAD) middle domain
This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold. [1]. 9129218. Peptidylarginine deiminase of the hair follicle:. characterization, localization, and function in keratinizing. tissues.. Rogers G, Winter B, McLaughlan C, Powell B, Nesci T;. J Invest Dermatol 1997;108:700-707.. [2]. 11166924. Protein deimination in the rat brain after kainate. administration: citrulline-containing proteins as a novel marker. of neurodegeneration.. Asaga H, Ishigami A;. Neurosci Lett 2001;299:5-8.. [3]. 10092850. Molecular cloning of cDNAs of mouse peptidylarginine deiminase. type I, type III and type IV, and the expression pattern of type. I in mouse.. Rus'd AA, Ikejiri Y, Ono H, Yonekawa T, Shiraiwa M, Kawada A,. Takahara H;. Eur J Biochem 1999;259:660-669. (from Pfam)
Protein-arginine deiminase (PAD) N-terminal domain
This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold. [1]. 9129218. Peptidylarginine deiminase of the hair follicle:. characterization, localization, and function in keratinizing. tissues.. Rogers G, Winter B, McLaughlan C, Powell B, Nesci T;. J Invest Dermatol 1997;108:700-707.. [2]. 11166924. Protein deimination in the rat brain after kainate. administration: citrulline-containing proteins as a novel marker. of neurodegeneration.. Asaga H, Ishigami A;. Neurosci Lett 2001;299:5-8.. [3]. 10092850. Molecular cloning of cDNAs of mouse peptidylarginine deiminase. type I, type III and type IV, and the expression pattern of type. I in mouse.. Rus'd AA, Ikejiri Y, Ono H, Yonekawa T, Shiraiwa M, Kawada A,. Takahara H;. Eur J Biochem 1999;259:660-669. (from Pfam)
bacteriocin immunity protein
Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species [1]. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc Pfam:PF10439). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin [2]. The C-terminal hair-pin recognises the C-terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates [3]. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, Pfam:PF01721. Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids [4]. [1]. 15753083. 1.6-Angstroms crystal structure of EntA-im. A bacterial immunity. protein conferring immunity to the antimicrobial activity of the. pediocin-like bacteriocin enterocin A.. Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J;. J Biol Chem. 2005;280:19045-19050.. [2]. 12427956. Comparative studies of immunity proteins of pediocin-like. bacteriocins.. Fimland G, Eijsink VG, Nissen-Meyer J;. Microbiology. 2002;148:3661-3670.. [3]. 17586105. Molecular dynamics simulation study of interaction between a. class IIa bacteriocin and its immunity protein.. Soliman W, Bhattacharjee S, Kaur K;. Biochim Biophys Acta. 2007;1774:1002-1013.. [4]. 15611086. The C-terminal domain of pediocin-like. TRUNCATED at 1650 bytes (from Pfam)
PMG protein
This family consists of several mouse anagen-specific protein mKAP13 (PMG1 and PMG2). PMG1 and 2 contain characteristic repeats reminiscent of the keratin-associated proteins (KAPs). Both genes are expressed in growing hair follicles in skin as well as in sebaceous and eccrine sweat glands. Interestingly, expression is also detected in the mammary epithelium where it is limited to the onset of the pubertal growth phase and is independent of ovarian hormones. Their broad, developmentally controlled expression pattern, together with their unique amino acid composition, demonstrate that pmg-1 and pmg-2 constitute a novel KAP gene family participating in the differentiation of all epithelial cells forming the epidermal appendages [1]. [1]. 10446281. Pmg-1 and pmg-2 constitute a novel family of KAP genes. differentially expressed during skin and mammary gland. development.. Kuhn F, Lassing C, Range A, Mueller M, Hunziker T, Ziemiecki A,. Andres AC;. Mech Dev 1999;86:193-196. (from Pfam)
Agouti protein
The agouti protein regulates pigmentation in the mouse hair follicle producing a black hair with a subapical yellow band. A highly homologous protein agouti signal protein (ASIP)is present in humans and is expressed at highest levels in adipose tissue where it may play a role in energy homeostasis and possibly human pigmentation [1] [2]. [1]. 11837451. Agouti: from mouse to man, from skin to fat.. Voisey J, van Daal A;. Pigment Cell Res 2002;15:10-18.. [2]. 11833005. A polymorphism in the agouti signaling protein gene is. associated with human pigmentation.. Kanetsky PA, Swoyer J, Panossian S, Holmes R, Guerry D, Rebbeck. TR;. Am J Hum Genet 2002;70:770-775. (from Pfam)
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain
This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast [1,2,3], which are involved in homotypic membrane fusion of the endoplasmic reticulum [3]. This domain binds GTP and forms dimers with other molecule for membrane tethering [3]. [1]. 9087433. The ROOT HAIR DEFECTIVE3 gene encodes an evolutionarily. conserved protein with GTP-binding motifs and is required for. regulated cell enlargement in Arabidopsis.. Wang H, Lockwood SK, Hoeltzel MF, Schiefelbein JW;. Genes Dev 1997;11:799-811.. [2]. 12427979. Function of a plant stress-induced gene, HVA22. Synthetic. enhancement screen with its yeast homolog reveals its role in. vesicular traffic.. Brands A, Ho TH;. Plant Physiol 2002;130:1121-1131.. [3]. 26370501. Structures of the yeast dynamin-like GTPase Sey1p provide. insight into homotypic ER fusion.. Yan L, Sun S, Wang W, Shi J, Hu X, Wang S, Su D, Rao Z, Hu J,. Lou Z;. J Cell Biol. 2015;210:961-972. (from Pfam)
GATA-type transcription activator, N-terminal
GATA transcription factors mediate cell differentiation in a diverse range of tissues. Mutation are often associated with certain congenital human disorders. The six classical vertebrate GATA proteins, GATA-1 to GATA-6, are highly homologous and have two tandem zinc fingers. The classical GATA transcription factors function transcription activators. In lower metazoans GATA proteins carry a single canonical zinc finger. This family represents the N-terminal domain of the family of GATA transcription activators. [1]. 12446778. Deletion of the GATA domain of TRPS1 causes an absence of facial. hair and provides new insights into the bone disorder in. inherited tricho-rhino-phalangeal syndromes.. Malik TH, Von Stechow D, Bronson RT, Shivdasani RA;. Mol Cell Biol 2002;22:8592-8600. (from Pfam)
Keratin, high-sulphur matrix protein
Family of Keratin, high-sulfur matrix proteins. The keratin products of mammalian epidermal derivatives such as wool and hair consist of microfibrils embedded in a rigid matrix of other proteins. The matrix proteins include the high-sulphur and high-tyrosine keratins, having molecular weights of 6-20 kDa, whereas microfibrils contain the larger, low-sulphur keratins (40-56 kDa) [1]. [1]. 4678578. The amino acid sequence of protein SCMK-B2C from the. high-sulphur fraction of wool keratin.. Elleman TC;. Biochem J 1972;128:1229-1239. (from Pfam)
Keratin, high sulfur B2 protein
High sulfur proteins are cysteine-rich proteins synthesised during the differentiation of hair matrix cells, and form hair fibres in association with hair keratin intermediate filaments [1]. This family has been divided up into four regions, with the second region containing 8 copies of a short repeat [1]. This family is also known as B2 or KAP1. [1]. 9524245. Structure and hair follicle-specific expression of genes. encoding the rat high sulfur protein B2 family.. Mitsui S, Ohuchi A, Adachi-Yamada T, Hotta M, Tsuboi R, Ogawa H;. Gene 1998;208:123-129. (from Pfam)
exosporium leader peptide-containing protein
This domain is found as a leader peptide in at least a subset of proteins targeted to the type of exosporium that occurs as the outermost layer of Bacillus anthracis, B. cereus, and B. thuringiensis spores. The exosporium consists of a basal layer and a nap of hair-like filaments. BclA, the major protein of the nap filaments, is targeted there by this leader peptide. In known examples of proteins in this family, the exosporium leader peptide is followed immediately by collagen-like Pro-rich tripeptide repeats. The last six residues of the seed alignment represent the first two PXG repeats.
RIPOR family protein
RIPOR family protein similar to human Rho family-interacting cell polarization regulator 2 (RIPOR2) that acts as an inhibitor of the small GTPase RHOA and plays several roles in the regulation of myoblast and hair cell differentiation, lymphocyte T proliferation and neutrophil polarization
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