K1C18_DANRE
ID K1C18_DANRE Reviewed; 431 AA.
AC Q7ZTS4; Q6P042; Q7ZT44;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Keratin, type I cytoskeletal 18;
DE AltName: Full=Cytokeratin-18;
DE Short=CK-18;
DE AltName: Full=Dorsal aorta proneprin kinesin-1;
DE AltName: Full=DreK18;
DE AltName: Full=Keratin-18;
DE Short=K18;
GN Name=krt18 {ECO:0000312|EMBL:AAH45869.1,
GN ECO:0000312|ZFIN:ZDB-GENE-030411-6};
GN Synonyms=dapk1 {ECO:0000312|EMBL:AAQ10781.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAH45869.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH45869.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH45869.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-182.
RC STRAIN=AB;
RA Clark M., Johnson S.L., Lehrach H., Lee R., Li F., Marra M., Eddy S.,
RA Hillier L., Kucaba T., Martin J., Beck C., Wylie T., Underwood K.,
RA Steptoe M., Theising B., Allen M., Bowers Y., Person B., Swaller T.,
RA Gibbons M., Pape D., Harvey N., Schurk R., Ritter E., Kohn S., Shin T.,
RA Jackson Y., Cardenas M., McCann R., Waterston R., Wilson R.;
RT "WashU Zebrafish EST Project 1998.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAD38146.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-431, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12558605; DOI=10.1046/j.1432-0436.2003.700607.x;
RA Schaffeld M., Knappe M., Hunzinger C., Markl J.;
RT "cDNA sequences of the authentic keratins 8 and 18 in zebrafish.";
RL Differentiation 71:73-82(2003).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=9662643; DOI=10.1007/s004410051112;
RA Conrad M., Lemb K., Schubert T., Markl J.;
RT "Biochemical identification and tissue-specific expression patterns of
RT keratins in the zebrafish Danio rerio.";
RL Cell Tissue Res. 293:195-205(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-13; SER-22 AND
RP SER-36, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: When phosphorylated, plays a role in filament reorganization.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Keratin-18 associates with keratin-8 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in simple epithelia such as intestinal
CC mucosa, bile duct, hepatocytes, renal tubules, endothelia, ocular lens
CC epithelium, and in a variety of mesenchymally-derived cells such as
CC blood vessel endothelia, pillar gill cells, optic nerve glial cells,
CC fibroblasts, interstitial cells, chondrocytes and ovarian theca cells.
CC Also expressed in epidermis, pharyngeal mucosa, mucosa of anterior
CC esophagus, gill mucosa and cornea. {ECO:0000269|PubMed:12558605,
CC ECO:0000269|PubMed:9662643}.
CC -!- PTM: Proteolytically cleaved by caspases during epithelial cell
CC apoptosis. {ECO:0000250}.
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; AF537368; AAQ10781.1; -; mRNA.
DR EMBL; BC045869; AAH45869.1; -; mRNA.
DR EMBL; BC065848; AAH65848.1; -; mRNA.
DR EMBL; BF157147; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ493269; CAD38146.1; -; mRNA.
DR RefSeq; NP_848524.1; NM_178437.2.
DR AlphaFoldDB; Q7ZTS4; -.
DR SMR; Q7ZTS4; -.
DR IntAct; Q7ZTS4; 1.
DR MINT; Q7ZTS4; -.
DR STRING; 7955.ENSDARP00000110768; -.
DR iPTMnet; Q7ZTS4; -.
DR PaxDb; Q7ZTS4; -.
DR PRIDE; Q7ZTS4; -.
DR Ensembl; ENSDART00000127667; ENSDARP00000110768; ENSDARG00000018404.
DR Ensembl; ENSDART00000183130; ENSDARP00000148009; ENSDARG00000109528.
DR GeneID; 352912; -.
DR KEGG; dre:352912; -.
DR CTD; 352912; -.
DR ZFIN; ZDB-GENE-030411-6; krt18a.1.
DR eggNOG; ENOG502QUS8; Eukaryota.
DR GeneTree; ENSGT00940000163961; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q7ZTS4; -.
DR OMA; YRASSIH; -.
DR OrthoDB; 711591at2759; -.
DR PhylomeDB; Q7ZTS4; -.
DR Reactome; R-DRE-6805567; Keratinization.
DR Reactome; R-DRE-6809371; Formation of the cornified envelope.
DR PRO; PR:Q7ZTS4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000018404; Expressed in gastrula and 20 other tissues.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR027695; Keratin-18.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR PANTHER; PTHR23239:SF349; PTHR23239:SF349; 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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT CHAIN 2..431
FT /note="Keratin, type I cytoskeletal 18"
FT /evidence="ECO:0000250|UniProtKB:P05783"
FT /id="PRO_0000289072"
FT DOMAIN 84..395
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..83
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 84..119
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 120..136
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 137..228
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 229..252
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 253..390
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 391..431
FT /note="Tail"
FT /evidence="ECO:0000255"
FT SITE 242..243
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250"
FT SITE 335
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 21
FT /note="V -> A (in Ref. 1; AAH45869)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> T (in Ref. 3; CAD38146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48631 MW; 851BDACDFC8896B7 CRC64;
MSLRTSYSVR SSTSQVPVSQ VSIKRTTNVP TYRAASIYGG AGGQGTRISS ASYSGVRSGL
GVPSMSSSIQ VSASGSTGEI MGNEKMAMQN LNDRLASYLE KVRILEQANS KLELKIREAL
EKRGPDVHDY SRFQPIVDEL RKKIFDATTN NARLVLQIDN ARLAADDFRV KYESELSIRQ
GVEADITGLR KVIDDTNLNR MNLESEIEAL KEELIFLKKN HDNEVMELRN QISQSGVQVD
VDAPKGQDLS QIMEEIRAKY EKMALKNQEE LKAWHESQIT EVQVQVTQNT EALQGARSEV
NELRRQIQTL EIELESQKNL KGSLEGTLRD TEMRYNMEIE NLNTIILQLE AELTQLRGNI
QHQTQEYEAL LNIKMKLEAE IATYRRLLDG GDFKLQDALE EQKKVKVMTV TQTLVDGKVV
SSSTETKERK L
