K2C1_RAT
ID K2C1_RAT Reviewed; 625 AA.
AC Q6IMF3; A1L113; Q63115;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Keratin, type II cytoskeletal 1;
DE AltName: Full=Cytokeratin-1;
DE Short=CK-1;
DE AltName: Full=Keratin-1;
DE Short=K1;
DE AltName: Full=Type-II keratin Kb1;
GN Name=Krt1 {ECO:0000250|UniProtKB:P04264};
GN Synonyms=Kb1 {ECO:0000312|RGD:1359664};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/NHsdMcwi; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000312|EMBL:CAA38577.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 459-625.
RC STRAIN=Wistar {ECO:0000312|EMBL:CAA38577.1};
RC TISSUE=Epidermis {ECO:0000312|EMBL:CAA38577.1};
RA Redfern C.P.F., Allen G.;
RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:DAA02055.1}
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: May regulate the activity of kinases such as PKC and SRC via
CC binding to integrin beta-1 (ITB1) and the receptor of activated protein
CC C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor
CC for kininogen-1/HMWK (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins (By
CC similarity). Heterodimer with KRT10 (By similarity). Two heterodimers
CC of KRT1 and KRT10 form a heterotetramer (By similarity). Forms a
CC heterodimer with KRT14; the interaction is more abundant in the absence
CC of KRT5 (By similarity). Interacts with ITGB1 in the presence of RACK1
CC and SRC, and with RACK1 (By similarity). Interacts with C1QBP; the
CC association represents a cell surface kininogen receptor (By
CC similarity). Interacts with EPPK1; interaction is dependent of higher-
CC order structure of intermediate filament (By similarity).
CC {ECO:0000250|UniProtKB:P04104, ECO:0000250|UniProtKB:P04264}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04264}.
CC Cytoplasm {ECO:0000250|UniProtKB:P04264}.
CC -!- PTM: Undergoes deimination of some arginine residues (citrullination).
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; AABR03057642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127464; AAI27465.1; -; mRNA.
DR EMBL; X54806; CAA38577.1; -; mRNA.
DR EMBL; BK001580; DAA02055.1; -; mRNA.
DR PIR; S21359; S21359.
DR RefSeq; NP_001008802.2; NM_001008802.2.
DR AlphaFoldDB; Q6IMF3; -.
DR SMR; Q6IMF3; -.
DR BioGRID; 256511; 4.
DR IntAct; Q6IMF3; 1.
DR STRING; 10116.ENSRNOP00000029276; -.
DR iPTMnet; Q6IMF3; -.
DR PhosphoSitePlus; Q6IMF3; -.
DR jPOST; Q6IMF3; -.
DR PaxDb; Q6IMF3; -.
DR PRIDE; Q6IMF3; -.
DR GeneID; 300250; -.
DR KEGG; rno:300250; -.
DR UCSC; RGD:1359664; rat.
DR CTD; 3848; -.
DR RGD; 1359664; Krt1.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR InParanoid; Q6IMF3; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; Q6IMF3; -.
DR TreeFam; TF317854; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IMF3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0045095; C:keratin filament; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; ISO:RGD.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032449; Keratin_2_1_tail.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR Pfam; PF16210; Keratin_2_tail; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Citrullination; Coiled coil; Cytoplasm;
KW Intermediate filament; Keratin; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..625
FT /note="Keratin, type II cytoskeletal 1"
FT /id="PRO_0000278098"
FT DOMAIN 179..492
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..178
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..214
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 215..233
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 234..325
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 326..349
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 350..488
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 489..625
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 496..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..319
FT /evidence="ECO:0000255"
FT COILED 388..475
FT /evidence="ECO:0000255"
FT COMPBIAS 496..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 432
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 275
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 517
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 574
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 596
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT CONFLICT 514
FT /note="T -> S (in Ref. 2; AAI27465)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> S (in Ref. 2; AAI27465)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="C -> G (in Ref. 2; AAI27465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 64831 MW; 790AAC59E2A2707B CRC64;
MSFQCSSRSL CRSGGGGGGR NFSSGSAGLV SFQRRSTSSS MRRSGGGGGG RFSGGGFCGS
SGGGFGSKSL VNLGGGRSIS ISVAGGGSSY GGGFGGGSYG GGSFGGGSFG GGVGGGFGGG
GFGGGGFGSG GGFGGGRFGG GFGPVCPPGG IQEVTINQSL LQPLNVEVDP QIQKVKSQER
EQIKSLNDKF ASFIDKVRFL EQQNQVLQTK WELLQQVDTS TRTQNLDPFF ESYISNLRRQ
VDSLKNDQSR MDSELKNMQD LVEEYRTKYE DEINKRTNAE NEFVTIKKDV DSAYMNKAEL
QARVDNLQQD IDFFSTLYQM ELSQMQTQIS ETNVVLSMDN NRTLDLDGII AEVKAQYDSI
CQRSKAEAET FYQSKYEELQ ITAGKHGDSV KNTKMEISEL NRVIQRLRSE IDSVKKQISQ
MQQNISDAEQ RGEKALKDAQ NKLNEIEDAL TQAKEELTRL LRDYQELMNT KLALDMEIAT
YRKLLEGEEI RMSGECTPNV SVSVSTSHTS MSGTSSRGGG RYGSGGGGGG GTYGGGSRGG
SYGGGSGGGS YGGCSSGGGS GGGSYGGGSS GGHRGGSGGG GGSSGGSYGG SSGGGRGGSS
SGGGVKSSGS SSVKFVSTTY SRGTN
