K1C12_RAT
ID K1C12_RAT Reviewed; 456 AA.
AC Q6IFW5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Keratin, type I cytoskeletal 12;
DE AltName: Full=Cytokeratin-12;
DE Short=CK-12;
DE AltName: Full=Keratin-12;
DE Short=K12;
DE AltName: Full=Type I keratin Ka12;
GN Name=Krt12 {ECO:0000250|UniProtKB:Q99456};
GN Synonyms=Ka12 {ECO:0000312|EMBL:DAA04467.1},
GN Krt1-12 {ECO:0000312|RGD:1304805};
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:DAA04467.1}
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: Involved in corneal epithelium organization, integrity and
CC corneal keratin expression. {ECO:0000250|UniProtKB:Q64291}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Keratin-3 associates with keratin-12 (By similarity). {ECO:0000250}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AABR03075828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK004033; DAA04467.1; -; mRNA.
DR RefSeq; NP_001008761.1; NM_001008761.1.
DR AlphaFoldDB; Q6IFW5; -.
DR SMR; Q6IFW5; -.
DR STRING; 10116.ENSRNOP00000016337; -.
DR jPOST; Q6IFW5; -.
DR PaxDb; Q6IFW5; -.
DR PRIDE; Q6IFW5; -.
DR GeneID; 360625; -.
DR KEGG; rno:360625; -.
DR CTD; 3859; -.
DR RGD; 1304805; Krt12.
DR eggNOG; ENOG502QTM6; Eukaryota.
DR InParanoid; Q6IFW5; -.
DR OrthoDB; 798081at2759; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IFW5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0061303; P:cornea development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0060429; P:epithelium development; ISO:RGD.
DR GO; GO:0002009; P:morphogenesis of an epithelium; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 2.
DR Pfam; PF00038; Filament; 2.
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..456
FT /note="Keratin, type I cytoskeletal 12"
FT /id="PRO_0000282956"
FT DOMAIN 115..402
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..114
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..150
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 154..171
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 172..263
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 264..286
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 287..397
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 398..456
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 405..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 48820 MW; 15E5B2653EB3599E CRC64;
MSLSVRTSAL SRRSSSQNGV AGRPWGASAS SVACGYGGTA SGFGVGCGGL LSAASMFGSS
SGFSGGSTGC SPGLGTAYGG PLGAGVGGMG IGGSSGGGSL CIFSGNDGGL LSGSEKETMQ
NLNDRLASYL GKVRALEEAN AELENKIREW YETRRTGDSG SQSDYSKYYP LIEDLKNKII
SASVSNAQLL LQIDNARLAA EDFRMKYENE LALRQTVEAD INGLRRVLDE LTLARADLEA
QTENLTEELA YMKKNHEEEL QSFQAGGPGE VNVEMDAAPG VDLTKSGELR KEINSNTEQL
QSSKSEVTDL KRMVQNLEIE LQSQLAMKSS LEGSLAETEG GYCCQLSQMQ QLIGSLEEQL
QQLRADAERQ NEDHQRLLGV KARLEMEIET YRRLLEGDTQ GDGFDESLSL TVSKPQAPSV
DSSKDPNKTR KIKTVVQEIV NGEVVSSQVQ ELEEAM
