ID   K1C14_CHICK             Reviewed;         467 AA.
AC   Q6PVZ1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Keratin, type I cytoskeletal 14;
DE   AltName: Full=Cytokeratin-14;
DE            Short=CK-14;
DE   AltName: Full=Keratin-14;
DE            Short=K14;
GN   Name=KRT14;
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:AAS92202.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Keratinocyte {ECO:0000269|PubMed:15157236};
RX   PubMed=15157236; DOI=10.1111/j.1432-0436.2004.07204002.x;
RA   Vanhoutteghem A., Londero T., Ghinea N., Djian P.;
RT   "Serial cultivation of chicken keratinocytes, a composite cell type that
RT   accumulates lipids and synthesizes a novel beta-keratin.";
RL   Differentiation 72:123-137(2004).
CC   -!- FUNCTION: The nonhelical tail domain is involved in promoting KRT5-
CC       KRT14 filaments to self-organize into large bundles and enhances the
CC       mechanical properties involved in resilience of keratin intermediate
CC       filaments in vitro. {ECO:0000250|UniProtKB:P02533}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000250|UniProtKB:Q61781}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02533}. Nucleus
CC       {ECO:0000250|UniProtKB:P02533}. Note=Expressed in both as a filamentous
CC       pattern. {ECO:0000250|UniProtKB:P02533}.
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis.
CC       {ECO:0000269|PubMed:15157236}.
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; AY574987; AAS92202.1; -; mRNA.
DR   RefSeq; NP_001001311.2; NM_001001311.2.
DR   AlphaFoldDB; Q6PVZ1; -.
DR   SMR; Q6PVZ1; -.
DR   STRING; 9031.ENSGALP00000006090; -.
DR   PaxDb; Q6PVZ1; -.
DR   GeneID; 408039; -.
DR   KEGG; gga:408039; -.
DR   CTD; 3861; -.
DR   VEuPathDB; HostDB:geneid_408039; -.
DR   eggNOG; ENOG502R8V7; Eukaryota.
DR   InParanoid; Q6PVZ1; -.
DR   OrthoDB; 798081at2759; -.
DR   PhylomeDB; Q6PVZ1; -.
DR   PRO; PR:Q6PVZ1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; ISS:UniProtKB.
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; 2.
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; Cytoplasm; Intermediate filament; Keratin; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..467
FT                   /note="Keratin, type I cytoskeletal 14"
FT                   /id="PRO_0000063656"
FT   DOMAIN          109..420
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..108
FT                   /note="Head"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..144
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          145..162
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          163..254
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          255..277
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          278..416
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          417..467
FT                   /note="Tail"
FT                   /evidence="ECO:0000250|UniProtKB:P02533"
FT   REGION          419..467
FT                   /note="Interaction with Type I keratins and keratin
FT                   filaments"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  50986 MW;  AA9E3E3046E5D3B9 CRC64;
     MSTTVRQFSS STSLKGLGGG SSRLSCGRAA GYQAPSVHGG SSSYSVSSRI VSGLGAGYGG
     GYCSSVGGGL GGGFGASYGA GYGAGFGGGF GAGFGGGFGG GDGILPAGEK ETMQNLNDRL
     AAYLDKVRAL EEANTDLEVK IREWYKKQGP GPERDYSPYY RTIEELRSKI LAATVENANI
     VLQIDNARLA ADDFRTKFET EQALRLSVEA DINGLRRVLD ELTLSRADLE MQIENLKEEL
     AYLKKNHEEE MNALRGQVGG EISVEMDAAP GIDLTKILAE MREQYESLAE KNRRDAEQWF
     FSKTEELNRE VAVNTEQLQS GKTEITELRR TIQSLEIDLQ SQLSTKAALE GTLADTEARY
     GTQLAQLQAL ITSVEEQLAE LRCDMERQNH EYRVLLDVKC RLEQEIATYR RLLEGEDAHI
     SSQYSSAMSS HSGRDAITTS RQVRTIVEEV QDGKVVSSRE QMALTTR