KR101_HUMAN
ID KR101_HUMAN Reviewed; 282 AA.
AC P60331; Q0VAR0; Q0VAR1;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Keratin-associated protein 10-1;
DE AltName: Full=High sulfur keratin-associated protein 10.1;
DE AltName: Full=Keratin-associated protein 10.1;
DE AltName: Full=Keratin-associated protein 18-1;
DE AltName: Full=Keratin-associated protein 18.1;
GN Name=KRTAP10-1; Synonyms=KAP10.1, KAP18-1, KRTAP10.1, KRTAP18-1, KRTAP18.1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS LEU-39 AND
RP MET-101.
RC TISSUE=Hair root;
RX PubMed=15028290; DOI=10.1016/j.ygeno.2003.09.024;
RA Shibuya K., Obayashi I., Asakawa S., Minoshima S., Kudoh J., Shimizu N.;
RT "A cluster of 21 keratin-associated protein genes within introns of another
RT gene on human chromosome 21q22.3.";
RL Genomics 83:679-693(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-39; MET-101;
RP GLN-241 AND LEU-280.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-282, AND TISSUE SPECIFICITY.
RC TISSUE=Scalp;
RX PubMed=14962103; DOI=10.1046/j.0022-202x.2003.22128.x;
RA Rogers M.A., Langbein L., Winter H., Beckmann I., Praetzel S.,
RA Schweizer J.;
RT "Hair keratin associated proteins: characterization of a second high sulfur
RT KAP gene domain on human chromosome 21.";
RL J. Invest. Dermatol. 122:147-158(2004).
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.
CC -!- SUBUNIT: Interacts with hair keratins.
CC -!- TISSUE SPECIFICITY: Restricted to a narrow region of the hair fiber
CC cuticle, lying approximately 20 cell layers above the apex of the
CC dermal papilla of the hair root; not detected in any other tissues.
CC {ECO:0000269|PubMed:14962103, ECO:0000269|PubMed:15028290}.
CC -!- SIMILARITY: Belongs to the KRTAP type 10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB076347; BAD01534.1; -; mRNA.
DR EMBL; AP001067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120959; AAI20960.1; -; mRNA.
DR EMBL; BC120960; AAI20961.1; -; mRNA.
DR EMBL; AJ566380; CAD97461.1; -; mRNA.
DR CCDS; CCDS42954.1; -.
DR RefSeq; NP_941964.2; NM_198691.2.
DR AlphaFoldDB; P60331; -.
DR BioGRID; 132128; 139.
DR IntAct; P60331; 6.
DR STRING; 9606.ENSP00000383226; -.
DR BioMuta; KRTAP10-1; -.
DR DMDM; 215274024; -.
DR MassIVE; P60331; -.
DR PaxDb; P60331; -.
DR PeptideAtlas; P60331; -.
DR PRIDE; P60331; -.
DR DNASU; 386677; -.
DR Ensembl; ENST00000400375.1; ENSP00000383226.1; ENSG00000215455.4.
DR GeneID; 386677; -.
DR KEGG; hsa:386677; -.
DR MANE-Select; ENST00000400375.1; ENSP00000383226.1; NM_198691.3; NP_941964.2.
DR UCSC; uc002zfh.2; human.
DR CTD; 386677; -.
DR DisGeNET; 386677; -.
DR GeneCards; KRTAP10-1; -.
DR HGNC; HGNC:22966; KRTAP10-1.
DR HPA; ENSG00000215455; Tissue enriched (skin).
DR neXtProt; NX_P60331; -.
DR OpenTargets; ENSG00000215455; -.
DR PharmGKB; PA134884303; -.
DR VEuPathDB; HostDB:ENSG00000215455; -.
DR eggNOG; KOG4726; Eukaryota.
DR GeneTree; ENSGT00940000158579; -.
DR HOGENOM; CLU_062832_0_0_1; -.
DR InParanoid; P60331; -.
DR OMA; CRQVCCV; -.
DR TreeFam; TF351356; -.
DR PathwayCommons; P60331; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR SignaLink; P60331; -.
DR BioGRID-ORCS; 386677; 33 hits in 986 CRISPR screens.
DR GenomeRNAi; 386677; -.
DR Pharos; P60331; Tdark.
DR PRO; PR:P60331; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P60331; protein.
DR Bgee; ENSG00000215455; Expressed in skin of abdomen and 4 other tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR InterPro; IPR002494; KAP.
DR PANTHER; PTHR23262; PTHR23262; 4.
DR Pfam; PF13885; Keratin_B2_2; 3.
PE 2: Evidence at transcript level;
KW Keratin; Reference proteome; Repeat.
FT CHAIN 1..282
FT /note="Keratin-associated protein 10-1"
FT /id="PRO_0000185209"
FT REPEAT 26..30
FT /note="1"
FT REPEAT 31..35
FT /note="2"
FT REPEAT 36..40
FT /note="3"
FT REPEAT 57..61
FT /note="4"
FT REPEAT 79..83
FT /note="5"
FT REPEAT 89..93
FT /note="6"
FT REPEAT 99..103
FT /note="7"
FT REPEAT 104..108
FT /note="8"
FT REPEAT 109..113
FT /note="9"
FT REPEAT 121..125
FT /note="10"
FT REPEAT 131..135
FT /note="11"
FT REPEAT 141..145
FT /note="12"
FT REPEAT 146..150
FT /note="13"
FT REPEAT 163..167
FT /note="14"
FT REPEAT 173..177
FT /note="15"
FT REPEAT 183..187
FT /note="16"
FT REPEAT 193..197
FT /note="17"
FT REPEAT 198..202
FT /note="18"
FT REPEAT 210..214
FT /note="19"
FT REPEAT 220..224
FT /note="20"
FT REPEAT 225..229
FT /note="21"
FT REPEAT 244..248
FT /note="22"
FT REPEAT 251..255
FT /note="23"
FT REPEAT 262..266
FT /note="24"
FT REGION 26..266
FT /note="24 X 5 AA repeats of C-C-X(3)"
FT VARIANT 39
FT /note="P -> L (in dbSNP:rs233320)"
FT /evidence="ECO:0000269|PubMed:15028290,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_017603"
FT VARIANT 101
FT /note="V -> M (in dbSNP:rs233319)"
FT /evidence="ECO:0000269|PubMed:15028290,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047502"
FT VARIANT 241
FT /note="R -> Q (in dbSNP:rs233317)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047503"
FT VARIANT 280
FT /note="P -> L (in dbSNP:rs233316)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047504"
FT CONFLICT 2
FT /note="A -> T (in Ref. 3; AAI20960)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="D -> S (in Ref. 1; BAD01534 and 3; AAI20960/
FT AAI20961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 28660 MW; 3312B39453544BDF CRC64;
MAASTMSVCS SACSDSWQVD ACPESCCEPH CCALSCCAPA PCLTLVCTPV SRVSSPCCQA
ACEPSPCQSG CTSSCTPSCC QQSSCQPACC TSSPCQQACC VPVCCKPVCC LPTCSKDSSS
CCQQSSCQPT CCASSSSQQS CCVPVCCKPV CYVPTCSEDS SSCCQQSSCH PACCTSSPCQ
QACCVPVRCK PVCCKPICCV PVCSGASTSC CQQSSCQPAC CTTSCCRPSS SVSLLCRPVC
RPACCMPVSS CCAPASSCQA SCCRPASCVS LLCRPACSRP AC
