ID A0A5F5Y1W5_FELCA Unreviewed; 260 AA.
AC A0A5F5Y1W5;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFCAP00000060306.1};
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:0000313|Ensembl:ENSFCAP00000060306.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000060306.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000060306.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000060306.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000060306.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000060306.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000060306.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: In the hair cortex, hair keratin intermediate filaments are
CC embedded in an interfilamentous matrix, consisting of hair keratin-
CC associated proteins (KRTAP), which are essential for the formation of a
CC rigid and resistant hair shaft through their extensive disulfide bond
CC cross-linking with abundant cysteine residues of hair keratins. The
CC matrix proteins include the high-sulfur and high-glycine-tyrosine
CC keratins. {ECO:0000256|ARBA:ARBA00003327}.
CC -!- SUBUNIT: Interacts with hair keratins. {ECO:0000256|ARBA:ARBA00011662}.
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DR EMBL; AANG04004523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A5F5Y1W5; -.
DR Ensembl; ENSFCAT00000043766.3; ENSFCAP00000060306.1; ENSFCAG00000034182.3.
DR GeneTree; ENSGT00940000163441; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000034182; Expressed in tip of external ear and 1 other cell type or tissue.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR InterPro; IPR002494; KAP.
DR PANTHER; PTHR23262; KERATIN ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23262:SF50; KERATIN-ASSOCIATED PROTEIN 10-4-RELATED; 1.
DR Pfam; PF13885; Keratin_B2_2; 2.
PE 4: Predicted;
KW Keratin {ECO:0000256|ARBA:ARBA00022744};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
SQ SEQUENCE 260 AA; 26607 MW; 2A4B1BABC855CE61 CRC64;
LSEKCCLFPT APAMAASTLS VCSSDLSYGS RVCLPGASDS CPDSSWQVDD CPESCCEPPC
CAPGDCCTPA CCKPVCCTPV CCKPVCCTPV CCKLFSCTPV CCEDSPCTTS SCCQPSCCTS
SPCQEDCCTP VCCKPVCCTP VCCEDSPCSA PSCCQPTSCV SLLCRPVCRP TCCTPVCCKP
VCCTPVCCED SPCSAPSCCQ PSPCCRPSSS VSLLCRPVCP RPACCAPASS CCRPASCVSL
LCRPVCPRPA CGPASGQSCC
//
