K2C1_PANTR
ID K2C1_PANTR Reviewed; 637 AA.
AC A5A6M6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Keratin, type II cytoskeletal 1 {ECO:0000250|UniProtKB:P04264};
DE AltName: Full=Cytokeratin-1 {ECO:0000250|UniProtKB:P04264};
DE Short=CK-1 {ECO:0000250|UniProtKB:P04264};
DE AltName: Full=Keratin-1;
DE Short=K1 {ECO:0000250|UniProtKB:P04264};
DE AltName: Full=Type-II keratin Kb1;
GN Name=KRT1 {ECO:0000312|EMBL:BAF62399.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1] {ECO:0000312|EMBL:BAF62399.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epidermis {ECO:0000269|PubMed:17574350};
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
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 {ECO:0000250|UniProtKB:P04264}.
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; AB222154; BAF62399.1; -; mRNA.
DR RefSeq; NP_001104288.1; NM_001110818.1.
DR AlphaFoldDB; A5A6M6; -.
DR SMR; A5A6M6; -.
DR PRIDE; A5A6M6; -.
DR GeneID; 738375; -.
DR KEGG; ptr:738375; -.
DR CTD; 3848; -.
DR InParanoid; A5A6M6; -.
DR OrthoDB; 824246at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
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..637
FT /note="Keratin, type II cytoskeletal 1"
FT /id="PRO_0000354095"
FT DOMAIN 175..488
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..174
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 22..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..210
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 211..229
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 230..321
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 322..345
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 346..484
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 484..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..637
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 563..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..323
FT /evidence="ECO:0000255"
FT COILED 384..473
FT /evidence="ECO:0000255"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 428
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 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 45
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 82
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 271
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04264"
FT MOD_RES 513
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
FT MOD_RES 583
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04104"
SQ SEQUENCE 637 AA; 65489 MW; 47E1C956C6C21D81 CRC64;
MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG
GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GSGIGGGGFG
GFGSGGGGFG GGGFGGGYGP VCPPGGIQEV TINQSLLQPL NVEIDPEIQK VKSREREQIK
SLNNQFASFI DKVRFLEQQN QVLQTKWELL QQVDTSTRTH NLEPYFESFI NNLRRRVDQL
KSDQSRLDSE LNNMQDMVED YRNKYEDEIN KRTNAENEFV TIKKDVDGAY MTKVDLQAKL
DNLQQEIDFL TALYQAELSQ MQTQISETNV ILSMDNNRSL DLDSIIAEVK AQYEDIAQKS
KAEAESLYQS KYEELQITAG RHGDSVRNSK IEISELNRVI QRLRSEIDNV KKQISNLQQS
ISDAEQRGEN ALKDAKNKLN DLEDALQQAK EDLARLLRDY QELMNTKLAL DLEIATYRTL
LEGEESRMSG ECAPNVGVSV STSHTTISGG GGRGGGGGGY GSGGSSYGSG GGSYGSGGGG
GGGRGSYGSG GSSYGSGGGS YGSGGGGGGH GSYGSGSSSG GYRGGSGGGG SSGGRGSGGG
SSGGSIGGRG SSSGGVKSSG GSSSVKFVST TYSGVTR
