ID Q64526_MOUSE Unreviewed; 186 AA.
AC Q64526;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=Keratin associated protein 9-1 {ECO:0000313|EMBL:AAI16211.1, ECO:0000313|Ensembl:ENSMUSP00000091468.4};
DE SubName: Full=Ultra-high sulphur keratin {ECO:0000313|EMBL:AAA81560.1};
GN Name=Krtap9-1 {ECO:0000313|EMBL:AAI16211.1,
GN ECO:0000313|Ensembl:ENSMUSP00000091468.4,
GN ECO:0000313|MGI:MGI:1309997};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAA81560.1};
RN [1] {ECO:0000313|EMBL:AAA81560.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2465353; DOI=10.1111/1523-1747.ep12276832;
RA McNab A.R., Wood L., Theriault N., Gierman T., Vogeli G.;
RT "An ultra-high sulfur keratin gene is expressed specifically during hair
RT growth.";
RL J. Invest. Dermatol. 92:263-266(1989).
RN [2] {ECO:0000313|EMBL:AAI16211.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI16211.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000091468.4, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000091468.4,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000091468.4}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000091468.4};
RG Ensembl;
RL Submitted (NOV-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; M27685; AAA81560.1; -; Genomic_DNA.
DR EMBL; BC116210; AAI16211.1; -; mRNA.
DR PIR; A45910; A45910.
DR RefSeq; NP_056556.1; NM_015741.2.
DR STRING; 10090.ENSMUSP00000091468; -.
DR PaxDb; 10090-ENSMUSP00000091468; -.
DR ProteomicsDB; 343213; -.
DR DNASU; 16705; -.
DR Ensembl; ENSMUST00000093936.5; ENSMUSP00000091468.4; ENSMUSG00000070335.5.
DR GeneID; 16705; -.
DR KEGG; mmu:16705; -.
DR UCSC; uc007ljv.2; mouse.
DR AGR; MGI:1309997; -.
DR CTD; 728318; -.
DR MGI; MGI:1309997; Krtap9-1.
DR VEuPathDB; HostDB:ENSMUSG00000070335; -.
DR eggNOG; KOG4726; Eukaryota.
DR GeneTree; ENSGT00940000159486; -.
DR HOGENOM; CLU_113141_0_0_1; -.
DR OMA; CCATRCV; -.
DR OrthoDB; 4851937at2759; -.
DR TreeFam; TF351356; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR BioGRID-ORCS; 16705; 3 hits in 56 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 11.
DR Bgee; ENSMUSG00000070335; Expressed in lip and 4 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR InterPro; IPR002494; KAP.
DR PANTHER; PTHR23262; KERATIN ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23262:SF32; KERATIN-ASSOCIATED PROTEIN 9-8; 1.
DR Pfam; PF13885; Keratin_B2_2; 3.
PE 1: Evidence at protein level;
KW Keratin {ECO:0000256|ARBA:ARBA00022744, ECO:0000313|EMBL:AAI16211.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q64526};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 186 AA; 19658 MW; 61D6BFDAB72CFEB4 CRC64;
MTNSCCSPCC QPTCCRTTCC RTTCWRPSCV TSCCQPCCQP SCCGSSCCQP CCQTTCCRTC
FQPCCVSSCC RTPCCQPCCC VSSCCQPCCQ PSCCQSSCCQ PRCCESSCCQ PRCCISSCCQ
PCCRPSCCQS SCCRPCCQPF CLNLCCQPAC SGPVTCTRTC YQPTCVCVPG CLSQGCGSSC
CEPCGC
//