ID   K118A_POLSE             Reviewed;         428 AA.
AC   A1KQY9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Keratin, type I cytoskeletal 18-A;
DE   AltName: Full=Cytokeratin-18-A;
DE            Short=CK-18-A;
DE   AltName: Full=Keratin-18-A;
DE            Short=K18-A;
GN   Name=krt18a {ECO:0000312|EMBL:CAL99126.1};
OS   Polypterus senegalus (Senegal bichir).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Polypteriformes; Polypteridae; Polypterus.
OX   NCBI_TaxID=55291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17553169; DOI=10.1186/1742-9994-4-16;
RA   Schaffeld M., Haberkamp M., Schatzlein S., Neumann S., Hunzinger C.;
RT   "A novel and ancient group of type I keratins with members in bichir,
RT   sturgeon and gar.";
RL   Front. Zool. 4:16-16(2007).
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   -!- PTM: Phosphorylated. {ECO:0000250}.
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; AM419448; CAL99126.1; -; mRNA.
DR   AlphaFoldDB; A1KQY9; -.
DR   SMR; A1KQY9; -.
DR   PRIDE; A1KQY9; -.
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; 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   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P05783"
FT   CHAIN           2..428
FT                   /note="Keratin, type I cytoskeletal 18-A"
FT                   /id="PRO_0000289074"
FT   DOMAIN          79..390
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          2..78
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          79..114
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          115..131
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          132..223
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          224..247
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          248..385
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          386..428
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   SITE            237..238
FT                   /note="Cleavage; by caspases"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  48527 MW;  1CF38B4A3C1BA7DB CRC64;
     MSFRSQTSST TSMRPVSSYS SRSISLHRSV PLGSSASVVG GAGGHGARIS SGGFGLASGY
     SSGSSFSMSV KGSGLFNNEK ETMQILNDRL ASYLETVRNL EQANSKLELQ IRETLEKRGP
     TTQDYSAYEK VVEDLKSQIY DMTVNNARLV LQIDNARLAT DDFRVKYESE LAIRQSVESD
     IIGLRKVIDD TNINRMNLET DIESLKEELI FIKRSHQTDV EELRKHISEC GVQVDVDAPK
     GQDLSKIMEE IRAQYETIIQ KNREELKDWH NSQILIVETE VKENTEALQK SRTEVTELRR
     QFQTLEIDIE SLRTMKASLE ANLHDVEMRN NMEMEGFNFI IRQQEADLQQ LRTSIQAQVH
     EYQALLNIKM KLEAEIATYR RLLDGEDFRL QDALAVQTTK VQKKITVTET VVDGKVVSQS
     SEVQEIKK