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K1C39_RAT
ID   K1C39_RAT               Reviewed;         481 AA.
AC   Q6IFW3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Keratin, type I cytoskeletal 39;
DE   AltName: Full=Cytokeratin-39;
DE            Short=CK-39;
DE   AltName: Full=Keratin-39;
DE            Short=K39;
DE   AltName: Full=Type I hair keratin Ka35;
GN   Name=Krt39; Synonyms=Ka35;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
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]
RP   IDENTIFICATION.
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: May play a role in late hair differentiation. {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa,
CC       respectively).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AABR03073663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK004035; DAA04469.1; -; mRNA.
DR   RefSeq; NP_001004130.1; NM_001004130.1.
DR   AlphaFoldDB; Q6IFW3; -.
DR   SMR; Q6IFW3; -.
DR   STRING; 10116.ENSRNOP00000039322; -.
DR   PaxDb; Q6IFW3; -.
DR   PRIDE; Q6IFW3; -.
DR   GeneID; 303523; -.
DR   KEGG; rno:303523; -.
DR   UCSC; RGD:1303032; rat.
DR   CTD; 390792; -.
DR   RGD; 1303032; Krt39.
DR   eggNOG; ENOG502SH7Y; Eukaryota.
DR   InParanoid; Q6IFW3; -.
DR   OrthoDB; 798081at2759; -.
DR   PhylomeDB; Q6IFW3; -.
DR   Reactome; R-RNO-6805567; Keratinization.
DR   Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR   PRO; PR:Q6IFW3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005882; C:intermediate filament; TAS:RGD.
DR   GO; GO:0045095; C:keratin filament; TAS:RGD.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS: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:0045103; P:intermediate filament-based process; TAS: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; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Keratin, type I cytoskeletal 39"
FT                   /id="PRO_0000314855"
FT   DOMAIN          90..401
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..90
FT                   /note="Head"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..125
FT                   /note="Coil 1A"
FT   REGION          126..136
FT                   /note="Linker 1"
FT   REGION          137..237
FT                   /note="Coil 1B"
FT   REGION          238..253
FT                   /note="Linker 12"
FT   REGION          254..397
FT                   /note="Coil 2"
FT   REGION          398..481
FT                   /note="Tail"
FT   SITE            339
FT                   /note="Stutter"
SQ   SEQUENCE   481 AA;  54338 MW;  5606D6E04F5CBB31 CRC64;
     MDTKGSTVTI SSSTPPQNCS GNTNVRTNSS NKSCYHDVQS TGHALQTPQG QGCRPSPCLY
     RCPNYLIRTY SFHPCPDDCS RCSDGINSHE KETMQILNER LASYLEKVRM LEGENADLED
     KIQEECSKTL PILCPDYLSY YTTIEQLQQK ILCTKAENSR LVSQIDNTKL AADDLRAKYE
     AELSLRQLVE ADANGLKQIL DALTLSKADL EARVQSLTEE LLCLKTNHEE EINSLQCQLG
     DRINIEVTAA PSVDLNQILQ KMRCQYESIV ETNRKDVEEW FNTQMEELNQ QVVSSSQQQQ
     CCQKDIIELR RTISALEVEL QAQHRMRDSQ ECILAETEAR YTALLAQIQS LIHNLEAQVA
     EIRSALQRQN QEYEVLLDIK SRLECEIATY RSLLESLDGR LPCNPCTTTW EPSCQARAME
     CLTPVYTSIS LPGIHKPCRA SGPPSRILVK ICTITKEIKD GKVISSHEHV QPCYITRPAK
     V
 
 
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