K1C19_CHICK
ID K1C19_CHICK Reviewed; 423 AA.
AC O93256;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Keratin, type I cytoskeletal 19;
DE AltName: Full=Cytokeratin-19;
DE Short=CK-19;
DE AltName: Full=GK-19;
DE AltName: Full=Keratin-19;
DE Short=K19;
GN Name=KRT19 {ECO:0000250|UniProtKB:P08727};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31952.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:9493835};
RX PubMed=9493835; DOI=10.1046/j.1440-169x.1997.t01-5-00011.x;
RA Sato K., Yasugi S.;
RT "Chicken keratin-19: cloning of cDNA and analysis of expression in the
RT chicken embryonic gut.";
RL Dev. Growth Differ. 39:751-761(1997).
CC -!- FUNCTION: Involved in the organization of myofibers. Together with
CC KRT8, helps to link the contractile apparatus to dystrophin at the
CC costameres of striated muscle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with PNN and the actin-binding domain of DMD (By similarity).
CC {ECO:0000250|UniProtKB:P08727, ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the digestive tract throughout
CC development in the epithelia of proventriculus and glandular
CC structures. In 13 day embryo, strongly expressed in esophagus with
CC moderate expression in proventriculus and lung. Weak expression in
CC gizzard, small intestine, lung and dorsal skin. In embryos over 13 days
CC old, observed in ectodermal, endodermal epithelium and also in neural
CC and mesodermal tissues (i.e. notochord), floorplate in the neural tube,
CC somatic mesoderm, splanchnic mesoderm and dermatome. In more developed
CC embryos, expression was localized in the anterior lobe of the pituitary
CC gland, notochord and hypothalamus of the diencephalon (derived from the
CC floor plate of the neural tube). Also localized in the mesonephric
CC mesoderm and lateral plate mesoderm. {ECO:0000269|PubMed:9493835}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain. {ECO:0000305}.
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; AB016281; BAA31952.1; -; mRNA.
DR RefSeq; NP_990340.2; NM_205009.2.
DR AlphaFoldDB; O93256; -.
DR SMR; O93256; -.
DR BioGRID; 676134; 1.
DR STRING; 9031.ENSGALP00000006093; -.
DR PaxDb; O93256; -.
DR PRIDE; O93256; -.
DR GeneID; 395861; -.
DR KEGG; gga:395861; -.
DR CTD; 192666; -.
DR VEuPathDB; HostDB:geneid_395861; -.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR InParanoid; O93256; -.
DR OrthoDB; 798081at2759; -.
DR PhylomeDB; O93256; -.
DR PRO; PR:O93256; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Coiled coil; Intermediate filament; Keratin; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..423
FT /note="Keratin, type I cytoskeletal 19"
FT /evidence="ECO:0000305"
FT /id="PRO_0000227527"
FT DOMAIN 94..405
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..93
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 94..129
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 130..147
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 148..239
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 240..262
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 258..415
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT REGION 263..401
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 402..414
FT /note="Rod-like helical tail"
FT /evidence="ECO:0000255"
FT REGION 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 281
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT SITE 341
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
SQ SEQUENCE 423 AA; 46082 MW; E03390A9558AD2D0 CRC64;
MATYSFRQTT SSVAGGPCGR SLRLGGGSFR APSIHGGSGG RGVSVSSARF VSSGLGSGLG
GGYGGAFSSS FSAGFGGGYG GGLGSGDGLL SGNEKTTMQN LNDRLASYLD KVRALEEANS
DLETKIREWY LKQGPGPARD YSPYYKAIED LRDQILAATI DNSKVVLQID NARLAADDFK
TKFETEQALR MSVEADINGL RRVLDELTLA RTDLELQIEN LKEELAYLKK NHEEEMSALG
GQVASQVSVE VDSAPGIDLS KILADMRDQY EHMAEKNRKD AEAWFHSKTE ELNRELAVNT
EQLQSSKSEV TDLRRTLQGL EIELQSQLSM KGALESTLAD TEGRYGAQLA QIQDMIGSIE
AQLAELRADM ERQNSEYKML MDIKTRLEQE IATYRQLLEG QESQLFGSLS GSPDKRDKPA
DGK
