K2C1B_RAT
ID K2C1B_RAT Reviewed; 519 AA.
AC Q6IG01;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Keratin, type II cytoskeletal 1b;
DE AltName: Full=Cytokeratin-1B;
DE Short=CK-1B;
DE AltName: Full=Keratin-77;
DE Short=K77;
DE AltName: Full=Type-II keratin Kb39;
GN Name=Krt77; Synonyms=Kb39, Krt1b;
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:DAA02229.1}
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 -!- PTM: Undergoes deimination of some arginine residues (citrullination).
CC {ECO:0000250|UniProtKB:Q6IFZ6}.
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; AABR03056255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03057642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK003984; DAA02229.1; -; mRNA.
DR RefSeq; NP_001008807.1; NM_001008807.1.
DR AlphaFoldDB; Q6IG01; -.
DR SMR; Q6IG01; -.
DR STRING; 10116.ENSRNOP00000052203; -.
DR iPTMnet; Q6IG01; -.
DR PhosphoSitePlus; Q6IG01; -.
DR jPOST; Q6IG01; -.
DR PaxDb; Q6IG01; -.
DR PRIDE; Q6IG01; -.
DR GeneID; 406226; -.
DR KEGG; rno:406226; -.
DR UCSC; RGD:1302968; rat.
DR CTD; 374454; -.
DR RGD; 1302968; Krt77.
DR eggNOG; ENOG502QQIF; Eukaryota.
DR HOGENOM; CLU_012560_6_1_1; -.
DR InParanoid; Q6IG01; -.
DR PhylomeDB; Q6IG01; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6IG01; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000036865; Expressed in heart and 5 other tissues.
DR ExpressionAtlas; Q6IG01; baseline and differential.
DR Genevisible; Q6IG01; RN.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Citrullination; Coiled coil; Intermediate filament; Keratin; Methylation;
KW Reference proteome.
FT CHAIN 1..519
FT /note="Keratin, type II cytoskeletal 1b"
FT /id="PRO_0000063713"
FT DOMAIN 167..480
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..166
FT /note="Head"
FT REGION 167..202
FT /note="Coil 1A"
FT REGION 203..221
FT /note="Linker 1"
FT REGION 222..313
FT /note="Coil 1B"
FT REGION 314..337
FT /note="Linker 12"
FT REGION 338..476
FT /note="Coil 2"
FT REGION 477..519
FT /note="Tail"
FT REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 420
FT /note="Stutter"
FT MOD_RES 81
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
FT MOD_RES 95
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6IFZ6"
SQ SEQUENCE 519 AA; 57255 MW; EE851CD1BB537055 CRC64;
MSRQFSSQSA FSSRSRRVYS TRSSSGFGGG RQILVSVGQS RRCGGDYGGG FSSRSLYSLG
GSKSIFGGLV GRSASGFCQS RGAGGGFGGG FGGGRSFGGG GFGGGYGGGG RFGGGFGGGF
GTSNFGLGGF GPSYPPGGIH EVTVNQSLLE PLHLEVDPEI QKIKTQEREQ IKTLNNKFAS
FIDKVRFLEQ QNQVLQTKWE LLQQVNTSTR TSSLEPIFEE FINQLQRQVD VLTNEQLRQN
SEIRSMQDIV EDYKNKYEDE INKRTNSEND FVVLKKDVDA AFMAKSDLQS RVDTLYGEIN
FLKYLFDTEL SQIQTHVSDT NVILSMDNNR SLDLDSIINA VRTQYELIAQ KSKDEAEALY
QTKYQELQIT AGKHGDDLKN SKMEISELNR NAQRLQAEIA NIKKQIEQMH GSISDAEERG
ERALQDAKQK LQETEEALQQ MKEDLARLLR DYQALLGAKL SLDVEIATYR ELLEGEESRM
SGALQSQVSI WALPSNEGND LGERLHDPQS QVPVPKLGC
