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K2C71_FELCA
ID   K2C71_FELCA             Reviewed;         524 AA.
AC   E1AB55;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Keratin, type II cytoskeletal 71;
DE   AltName: Full=Cytokeratin-71;
DE            Short=CK-71;
DE   AltName: Full=Keratin-71;
DE            Short=K71;
GN   Name=KRT71;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000312|EMBL:ADM23868.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-439, AND POLYMORPHISM.
RX   PubMed=20953787; DOI=10.1007/s00335-010-9290-6;
RA   Gandolfi B., Outerbridge C.A., Beresford L.G., Myers J.A., Pimentel M.,
RA   Alhaddad H., Grahn J.C., Grahn R.A., Lyons L.A.;
RT   "The naked truth: Sphynx and Devon Rex cat breed mutations in KRT71.";
RL   Mamm. Genome 21:509-515(2010).
CC   -!- FUNCTION: Plays a central role in hair formation. Essential component
CC       of keratin intermediate filaments in the inner root sheath (IRS) of the
CC       hair follicle. {ECO:0000250|UniProtKB:Q3SY84}.
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Associates with
CC       KRT16 and/or KRT17 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q3SY84}.
CC   -!- POLYMORPHISM: A complex variation, consisting of an 81-bp deletion,
CC       including the last 4 bp of intron 6 and the first 77 bp of exon 7,
CC       followed by 2 insertions was identified. This variation was called Rex
CC       polymorphism or 'Re'. All sequenced Devon Rex cats, a breed
CC       characterized by curly hair phenotype, were homozygous for this
CC       variation and loss of homozygosity was associated with normal hair
CC       production (PubMed:20953787). A variation affecting the 5'-splice site
CC       at the junction of exon 4 and intron 4 was identified in 2 breeds,
CC       Sphynx and Kohana, that are characterized by a hairless phenotype. This
CC       variation occurred in the heterozygous or homozygous state in these
CC       breeds. It has been called hairless or hr allele and has been suggested
CC       of a cause of the hairless phenotype (PubMed:20953787).
CC       {ECO:0000269|PubMed:20953787}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family. {ECO:0000305}.
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DR   EMBL; HM564031; ADM23868.1; -; mRNA.
DR   RefSeq; NP_001182168.1; NM_001195239.1.
DR   AlphaFoldDB; E1AB55; -.
DR   SMR; E1AB55; -.
DR   GeneID; 100500727; -.
DR   KEGG; fca:100500727; -.
DR   CTD; 112802; -.
DR   eggNOG; ENOG502SK67; Eukaryota.
DR   HOGENOM; CLU_012560_6_1_1; -.
DR   InParanoid; E1AB55; -.
DR   OMA; GPVCSTV; -.
DR   OrthoDB; 671547at2759; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
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; Cytoskeleton; Intermediate filament; Keratin;
KW   Reference proteome.
FT   CHAIN           1..524
FT                   /note="Keratin, type II cytoskeletal 71"
FT                   /id="PRO_0000452323"
FT   DOMAIN          131..444
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..130
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          131..166
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          167..185
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          186..277
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          278..301
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          302..440
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          441..524
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   REGION          491..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            382
FT                   /note="Stutter"
FT                   /evidence="ECO:0000255"
FT   VARIANT         439
FT                   /note="S -> G"
FT                   /evidence="ECO:0000269|PubMed:20953787"
SQ   SEQUENCE   524 AA;  57301 MW;  74DFD14E5D5C66CD CRC64;
     MNRQFTCKSG AAAKGGFSGC SAVLSGGSSS SYRAGGKGLS GGFGSRSLYS LGGIRNISLN
     MASGSGKSGY GFGRGRASGF AGSMFGSVAL GPVCPTVCPP GGIHQVTVNE SLLAPLNVEL
     DPEIQKVRAQ EREQIKALNN KFASFIDKVR FLEQQNQVLE TKWELLQQLD LNNCKNNLEP
     ILEGYISNLR KQLETLSGDR VRLDSELRSV RDVVEDYKKK YEEEINRRTA AENEFVLLKK
     DVDAAYANKE ELQAKVDSMD QEIKFFKCLY EAEIAQIQSH ISDMSVILSM DNNRDLNLDS
     IIDEVRAQYE EIALKSKAEA EALYQTKFQE LQLAAGRHGD DLKNTKNEIS ELTRLIQRIR
     SEIENVKKQA SNLETAIADA EQRGDSALKD ARAKLDELES ALHQAKEELA RMLREYQELM
     SLKLALDMEI ATYRKLLESE ECRMSGEFPS PVSISIISST SGSSGYGLRP SSVSGGYVAN
     SSSCISGVCS VRGGEGRSRG STSDYKDTLG KGSSQSASSK KASR
 
 
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