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K1C13_RAT
ID   K1C13_RAT               Reviewed;         438 AA.
AC   Q6IFV4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Keratin, type I cytoskeletal 13;
DE   AltName: Full=Cytokeratin-13;
DE            Short=CK-13;
DE   AltName: Full=Keratin-13;
DE            Short=K13;
DE   AltName: Full=Type I keratin Ka13;
GN   Name=Krt13 {ECO:0000250|UniProtKB:P13646};
GN   Synonyms=Ka13 {ECO:0000312|EMBL:DAA04478.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:DAA04478.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000312|EMBL:DAA04478.1};
RX   PubMed=15085952; DOI=10.1078/0171-9335-00354;
RA   Hesse M., Zimek A., Weber K., Magin T.M.;
RT   "Comprehensive analysis of keratin gene clusters in humans and rodents.";
RL   Eur. J. Cell Biol. 83:19-26(2004).
CC   -!- FUNCTION: Type 1 keratin (Probable). Maintains postnatal tongue mucosal
CC       cell homeostasis and tissue organization in response to mechanical
CC       stress, potentially via regulation of the G1/S phase cyclins CCNE1 and
CC       CCNE2 (By similarity). {ECO:0000250|UniProtKB:P08730, ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
CC   -!- PTM: O-glycosylated; glycans consist of single N-acetylglucosamine
CC       residues. {ECO:0000250|UniProtKB:P13646}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AABR03073341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK004044; DAA04478.1; -; mRNA.
DR   RefSeq; NP_001004021.1; NM_001004021.1.
DR   AlphaFoldDB; Q6IFV4; -.
DR   SMR; Q6IFV4; -.
DR   STRING; 10116.ENSRNOP00000018851; -.
DR   PhosphoSitePlus; Q6IFV4; -.
DR   jPOST; Q6IFV4; -.
DR   PaxDb; Q6IFV4; -.
DR   PRIDE; Q6IFV4; -.
DR   Ensembl; ENSRNOT00000018851; ENSRNOP00000018851; ENSRNOG00000014070.
DR   GeneID; 287699; -.
DR   KEGG; rno:287699; -.
DR   UCSC; RGD:1302937; rat.
DR   CTD; 3860; -.
DR   RGD; 1302937; Krt13.
DR   eggNOG; ENOG502QTM6; Eukaryota.
DR   GeneTree; ENSGT00940000154403; -.
DR   HOGENOM; CLU_012560_8_3_1; -.
DR   InParanoid; Q6IFV4; -.
DR   OMA; DAKMTGF; -.
DR   OrthoDB; 798081at2759; -.
DR   PhylomeDB; Q6IFV4; -.
DR   TreeFam; TF332742; -.
DR   Reactome; R-RNO-6805567; Keratinization.
DR   Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR   PRO; PR:Q6IFV4; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000014070; Expressed in esophagus and 13 other tissues.
DR   Genevisible; Q6IFV4; RN.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0045095; C:keratin filament; ISO:RGD.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR   GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0043555; P:regulation of translation in response to stress; ISS:UniProtKB.
DR   GO; GO:0009314; P:response to radiation; IEP:RGD.
DR   GO; GO:0043587; P:tongue morphogenesis; IEP:RGD.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Glycoprotein; Intermediate filament; Keratin; Methylation;
KW   Reference proteome.
FT   CHAIN           1..438
FT                   /note="Keratin, type I cytoskeletal 13"
FT                   /id="PRO_0000063649"
FT   DOMAIN          96..408
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..95
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          96..131
FT                   /note="Coil"
FT                   /evidence="ECO:0000255"
FT   REGION          132..150
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          151..242
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          243..265
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          266..404
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          405..438
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          408..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P13646"
FT   MOD_RES         35
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P13646"
SQ   SEQUENCE   438 AA;  47729 MW;  CFCE10BC2431519A CRC64;
     MSCRFQSSSM SYGGGFGAGS CQLGGGRNIS TCSSRFVTGG SSGGYGGGMS CGFGGGAGGG
     YGGGFGGGFG GSCGGGFGGG FGDFGSVDGG LLSGNEKITM QNLNDRLASY LEKVRALEAA
     NADLEVKIRD WHLKQSPTSP ERDYSAYYKT IEELRIKILE ATTDNNRIVL EIDNARLAAD
     DFRLKYENEL ALRQSVEADI NGLRRVLDEL TLAKTDLEMQ IESLNEELAY LKKNHEEEMK
     EFSNQAVGQV NVEMDATPGI DLTRVLAEMR EQYEALAEKN RRDAEAWFQA KSAELNKEVS
     SNAAMIQTSK TEITELRRTL QGLEIELQSQ LSMKAGLEST LAETECRYAL QLQQIQALIS
     SIEAQLSELR SEMECQNQEY KMLLDIKTRL EQEIATYRSL LEGQDAKMTG FNTGGNSTTT
     SNTSTSPSTS GRPDFRKY
 
 
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