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K1H2_MOUSE
ID   K1H2_MOUSE              Reviewed;         407 AA.
AC   Q62168; Q148N4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Keratin, type I cuticular Ha2;
DE   AltName: Full=Hair keratin, type I Ha2;
DE   AltName: Full=Keratin-32;
DE            Short=K32;
GN   Name=Krt32; Synonyms=Hka2, Krt1-2, Krtha2;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NMRI; TISSUE=Hair;
RX   PubMed=7514534; DOI=10.1006/excr.1994.1134;
RA   Winter H., Siry P., Tobiasch E., Schweizer J.;
RT   "Sequence and expression of murine type I hair keratins mHa2 and mHa3.";
RL   Exp. Cell Res. 212:190-200(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- TISSUE SPECIFICITY: Cuticle of the hair shaft.
CC   -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I
CC       (acidic) and II (neutral to basic).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; X75649; CAA53304.1; -; mRNA.
DR   EMBL; CH466662; EDL02584.1; -; Genomic_DNA.
DR   EMBL; BC117553; AAI17554.1; -; mRNA.
DR   EMBL; BC118064; AAI18065.1; -; mRNA.
DR   PIR; I48739; I48739.
DR   RefSeq; NP_001152846.2; NM_001159374.2.
DR   AlphaFoldDB; Q62168; -.
DR   SMR; Q62168; -.
DR   BioGRID; 201025; 2.
DR   STRING; 10090.ENSMUSP00000103042; -.
DR   iPTMnet; Q62168; -.
DR   PhosphoSitePlus; Q62168; -.
DR   jPOST; Q62168; -.
DR   MaxQB; Q62168; -.
DR   PaxDb; Q62168; -.
DR   PRIDE; Q62168; -.
DR   ProteomicsDB; 269443; -.
DR   DNASU; 16670; -.
DR   GeneID; 16670; -.
DR   KEGG; mmu:16670; -.
DR   CTD; 3882; -.
DR   MGI; MGI:1309995; Krt32.
DR   eggNOG; ENOG502SJJS; Eukaryota.
DR   InParanoid; Q62168; -.
DR   OrthoDB; 798081at2759; -.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 16670; 2 hits in 68 CRISPR screens.
DR   ChiTaRS; Krt32; mouse.
DR   PRO; PR:Q62168; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q62168; protein.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..407
FT                   /note="Keratin, type I cuticular Ha2"
FT                   /id="PRO_0000063687"
FT   DOMAIN          55..366
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..55
FT                   /note="Head"
FT   REGION          56..90
FT                   /note="Coil 1A"
FT   REGION          91..101
FT                   /note="Linker 1"
FT   REGION          102..202
FT                   /note="Coil 1B"
FT   REGION          203..218
FT                   /note="Linker 12"
FT   REGION          219..362
FT                   /note="Coil 2"
FT   REGION          363..407
FT                   /note="Tail"
FT   SITE            304
FT                   /note="Stutter"
FT   CONFLICT        227
FT                   /note="M -> V (in Ref. 1; CAA53304)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  46422 MW;  32D4D9FC1F1D642B CRC64;
     MPSVCMPTTY RPASCLSKTY LSSSCQPSNR RPTGCISSSM GTYGLFCEGA FNGNEKETMQ
     VLNDRLANYL EKVRQLEKEN AELEGKIQDV YQGQVLTMCP DYQSYFQTIE ELQQKVLCTK
     AENARMIVHI DNAKLAADDF RTKYETELAL RQLVEADTNG LRRILDELTL NKADLEAQVE
     SLKEELLCLK RNHEEEVGVL RQQLGDRLNI EVDAAPPVDL TRMLEEMRCQ YETMVETNHR
     DVEEWFNMQM EELNKQVATS SEQLQSYQSD IIDLRRTVNT LEIELQAQHS LRDSLENTLG
     ETEGRFTSQL SQMQCMITNV ESQLSDIRCD LERQNQEYKV LLDVKARLEC EIDTYRGLLE
     SEDSKLPCNP CSTPSCQPCA PSPGVSRTVC VPHTVCVPCS PCLQTRY
 
 
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