ID A0A452SC98_URSAM Unreviewed; 588 AA.
AC A0A452SC98;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Keratin, type II cytoskeletal 1 {ECO:0000256|ARBA:ARBA00015703};
DE AltName: Full=Cytokeratin-1 {ECO:0000256|ARBA:ARBA00032346};
DE AltName: Full=Keratin-1 {ECO:0000256|ARBA:ARBA00032123};
DE AltName: Full=Type-II keratin Kb1 {ECO:0000256|ARBA:ARBA00033007};
GN Name=KRT1 {ECO:0000313|Ensembl:ENSUAMP00000029944.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000029944.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000029944.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR AlphaFoldDB; A0A452SC98; -.
DR STRING; 9643.ENSUAMP00000029944; -.
DR Ensembl; ENSUAMT00000033412.1; ENSUAMP00000029944.1; ENSUAMG00000023016.1.
DR GeneTree; ENSGT00940000162175; -.
DR OMA; FGMAPGK; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045095; C:keratin filament; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IEA:Ensembl.
DR GO; GO:0001867; P:complement activation, lectin pathway; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
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 PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45616:SF33; KERATIN, TYPE II CYTOSKELETAL 1; 1.
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 SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Citrullination {ECO:0000256|ARBA:ARBA00022934};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685}; Keratin {ECO:0000256|ARBA:ARBA00022744};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT DOMAIN 163..476
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 218..308
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 338..454
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 61210 MW; 924E94FD7D7B7A08 CRC64;
MSRHFSSRSG LRSGGGFSSG SAGVVSFQRR TTSSSVRHGG GGGGRFSGGR CGGGGGGGGG
FGSRSLVNLG GSKSISISVA RGGGRGGFGG GYGGGGFGGF GSGGGFGGGG FGGGGFGGGG
FGGGSFGPVC PPGGIQEVTI NQSLLQPLNV EIDPEIQKVK TREREQIKSL NNQFASFIDK
VRFLEQQNQV LQTKWELLQQ VDTTTRTHNL EPYFESYINN LRRRVDQLKS DQSRMDSELK
NMQDLVEDYR NKYEDEINKR TNAENEFVTI KKDVDAAYMT KVDLQAKVDN LQQEIDFLTA
LYQAELSQMQ TQISETNVIL SMDNNRNLDL DSIIAEVKAQ YEEIAQKSKA EAEALYQTKY
EELQITAGKH GDNLKSTKME ISELNRVAQR LRSEIDSVKK QISALQQSIS DAEQRGENAL
KDAQGKLAEL EDALQKAKED LARLLRDYQE LMNTKLALDM EIATYRTLLE GEETVNTSHT
TISGGGGRGG GGFGSGGGGG YGSGGVSYGS GGSSYGSGGG GGGSYGSGGG GGYGSGSSSG
GHRGGSGGGG WGSGGSSGGR GSSSGGTKSS SGSSSVKFVS TSYSRAVR
//
