K1C13_PROAT
ID K1C13_PROAT Reviewed; 465 AA.
AC Q5K2P4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Keratin, type I cytoskeletal 13;
DE AltName: Full=Cytokeratin-13;
DE Short=CK-13;
DE AltName: Full=Keratin-13;
DE Short=K13;
GN Name=KRT13;
OS Protopterus aethiopicus (Marbled lungfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC Protopterus.
OX NCBI_TaxID=7886;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAH05043.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Skin {ECO:0000269|PubMed:15819414};
RX PubMed=15819414; DOI=10.1016/j.ejcb.2004.12.006;
RA Schaffeld M., Bremer M., Hunzinger C., Markl J.;
RT "Evolution of tissue-specific keratins as deduced from novel cDNA sequences
RT of the lungfish Protopterus aethiopicus.";
RL Eur. J. Cell Biol. 84:363-377(2005).
CC -!- FUNCTION: Type 1 keratin (Probable). May maintain oral mucosal cell
CC homeostasis and tissue organization in response to mechanical stress
CC (By similarity). {ECO:0000250|UniProtKB:P08730, ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in skin. {ECO:0000269|PubMed:15819414}.
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; AJ785787; CAH05043.1; -; mRNA.
DR AlphaFoldDB; Q5K2P4; -.
DR SMR; Q5K2P4; -.
DR PRIDE; Q5K2P4; -.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Intermediate filament; Keratin.
FT CHAIN 1..465
FT /note="Keratin, type I cytoskeletal 13"
FT /id="PRO_0000063651"
FT DOMAIN 100..412
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..98
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..135
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 136..154
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 155..246
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 247..269
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 270..408
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 409..465
FT /note="Tail"
FT /evidence="ECO:0000255"
SQ SEQUENCE 465 AA; 52348 MW; 8937B12A0DEC1D7D CRC64;
MNFTSFSITQ GSRPQPPSTR GFSGNSFKSD LIPQSRRSHS VYGTPGSIRI SSPSVPSAIV
SSYSSTLSSA LPSSSYGGNS FSSSTSFSSG GSDLLLGTSG KEAMQNLNDR LASYLEKVRS
LEERNRELEQ KIREWYEKQG AGTKTKDFSH YFKIIADLQK QIHDGNMENA KILLRIDNAK
LAADDFKQKW EAEQVMRLNV EGDINGLRRI LDEMTLARAD LEMQIDGQKE ELAYLNKSHD
EEMKALRSQL GGQVNVEVDA APAEDLTKKL ERMRQQYEQL AEKNRKDAED WFMKASEDLN
KNVASSTEAI QTTKTEINEL KRTIQGLQIE LQSQLSMKDA LEGQLADTEH RYSSILMNLQ
NIIHQKEAEL SDIRADTERQ ANEYKILFDA KTKLENEIRT YRILLEGDEG KFQTSPHHPS
IVTKQTETVV TPVVITNVKT VVEEIIDGKI VSKKEYPGPP EKLMI
