KRA51_MOUSE
ID KRA51_MOUSE Reviewed; 230 AA.
AC Q64507; A4IF43;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Keratin-associated protein 5-1 {ECO:0000250|UniProtKB:Q6L8H4};
DE AltName: Full=Ultra high sulfur serine protein 1;
DE Short=UHS-Ser-1;
GN Name=Krtap5-1 {ECO:0000312|MGI:MGI:1354732};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA40106.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAA40106.1};
RX PubMed=2250030; DOI=10.1016/s0021-9258(17)45371-3;
RA Wood L., Mills M., Hatzenbuhler N., Vogeli G.;
RT "Serine-rich ultra high sulfur protein gene expression in murine hair and
RT skin during the hair cycle.";
RL J. Biol. Chem. 265:21375-21380(1990).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI04356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
CC -!- FUNCTION: In the hair cortex, hair keratin intermediate filaments are
CC embedded in an interfilamentous matrix, consisting of hair keratin-
CC associated protein (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:0000305}.
CC -!- SUBUNIT: Interacts with hair keratins. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:2250030};
CC IsoId=Q64507-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q64507-2; Sequence=VSP_052994;
CC -!- TISSUE SPECIFICITY: Expressed during the active phases of the hair
CC cycle in the medulla and the inner root sheath of the forming hair.
CC Also expressed in the upper layers of the epidermis of skin.
CC {ECO:0000269|PubMed:2250030}.
CC -!- SIMILARITY: Belongs to the KRTAP type 5 family.
CC {ECO:0000250|UniProtKB:Q6L8H4}.
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DR EMBL; M37759; AAA40106.1; -; Genomic_DNA.
DR EMBL; BC104355; AAI04356.1; -; mRNA.
DR CCDS; CCDS80834.1; -. [Q64507-1]
DR PIR; A38346; A38346.
DR RefSeq; NP_056623.1; NM_015808.1. [Q64507-1]
DR AlphaFoldDB; Q64507; -.
DR DIP; DIP-112N; -.
DR STRING; 10090.ENSMUSP00000139752; -.
DR PhosphoSitePlus; Q64507; -.
DR PRIDE; Q64507; -.
DR DNASU; 50774; -.
DR Ensembl; ENSMUST00000188274; ENSMUSP00000139752; ENSMUSG00000066100. [Q64507-1]
DR GeneID; 50774; -.
DR KEGG; mmu:50774; -.
DR UCSC; uc009kmr.1; mouse. [Q64507-1]
DR CTD; 387264; -.
DR MGI; MGI:1354732; Krtap5-1.
DR VEuPathDB; HostDB:ENSMUSG00000066100; -.
DR eggNOG; KOG4726; Eukaryota.
DR GeneTree; ENSGT00940000164129; -.
DR OMA; CEAICCK; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR BioGRID-ORCS; 50774; 8 hits in 34 CRISPR screens.
DR ChiTaRS; Krtap5-1; mouse.
DR PRO; PR:Q64507; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q64507; protein.
DR Bgee; ENSMUSG00000066100; Expressed in lip and 5 other tissues.
DR ExpressionAtlas; Q64507; baseline and differential.
DR Genevisible; Q64507; MM.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR InterPro; IPR002494; KAP.
DR PANTHER; PTHR23262; PTHR23262; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Keratin; Reference proteome; Repeat.
FT CHAIN 1..230
FT /note="Keratin-associated protein 5-1"
FT /id="PRO_0000361657"
FT REPEAT 42..45
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 48..51
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 54..57
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 88..91
FT /note="4"
FT /evidence="ECO:0000255"
FT REPEAT 94..97
FT /note="5"
FT /evidence="ECO:0000255"
FT REPEAT 116..119
FT /note="6"
FT /evidence="ECO:0000255"
FT REPEAT 134..137
FT /note="7"
FT /evidence="ECO:0000255"
FT REPEAT 144..147
FT /note="8"
FT /evidence="ECO:0000255"
FT REPEAT 154..157
FT /note="9"
FT /evidence="ECO:0000255"
FT REPEAT 172..175
FT /note="10"
FT /evidence="ECO:0000255"
FT REPEAT 182..185
FT /note="11"
FT /evidence="ECO:0000255"
FT REPEAT 192..195
FT /note="12"
FT /evidence="ECO:0000255"
FT REPEAT 202..205
FT /note="13"
FT /evidence="ECO:0000255"
FT REPEAT 212..215
FT /note="14"
FT /evidence="ECO:0000255"
FT REGION 42..215
FT /note="14 X 4 AA repeats of C-C-X-P"
FT /evidence="ECO:0000255"
FT VAR_SEQ 150..217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052994"
FT CONFLICT 132
FT /note="S -> D (in Ref. 2; AAI04356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 21782 MW; 6CC50B41B2137C23 CRC64;
MTCCGCSGGC GSSCGGCGSS CGGCGSGCGG CGSNCGGCGS SCCKPVCCCK PVCCCVPVCS
CSSCGGCGSS CGGCGSCGSS CGGCGSSCCK PVCCCVPVCS CSSCGGCKPC CCQSSCCKPC
CSSGCGSSCC QSSCCKPCCC QSSCCKPCCC QSSCCKPCCS SGCGSSCCQS SCCKPCCCQS
SCCKPCCCQS SCCKPCCCQS SCCKPCCCQS SCCKPCCSSG CGSSCCQDSC