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CRIP1_MOUSE
ID   CRIP1_MOUSE             Reviewed;          77 AA.
AC   P63254; P04006; Q3THF0;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cysteine-rich protein 1;
DE            Short=CRP-1;
DE   AltName: Full=Cysteine-rich intestinal protein;
DE            Short=CRIP;
GN   Name=Crip1; Synonyms=Crip;
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].
RX   PubMed=3085096; DOI=10.1073/pnas.83.8.2516;
RA   Birkenmeier E.H., Gordon J.I.;
RT   "Developmental regulation of a gene that encodes a cysteine-rich intestinal
RT   protein and maps near the murine immunoglobulin heavy chain locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:2516-2520(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129S1/Sv;
RX   PubMed=12370427; DOI=10.1073/pnas.212392399;
RA   Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R.,
RA   Schildkraut C.L., Birshtein B.K.;
RT   "The origin of a developmentally regulated Igh replicon is located near the
RT   border of regulatory domains for Igh replication and expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Small intestine, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, and Spleen;
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).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-68, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Seems to have a role in zinc absorption and may function as
CC       an intracellular zinc transport protein.
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DR   EMBL; M13018; AAA37458.1; -; mRNA.
DR   EMBL; AF450245; AAM97585.1; -; Genomic_DNA.
DR   EMBL; AK003075; BAB22550.1; -; mRNA.
DR   EMBL; AK008269; BAB25566.1; -; mRNA.
DR   EMBL; AK012068; BAB28006.1; -; mRNA.
DR   EMBL; AK168305; BAE40246.1; -; mRNA.
DR   EMBL; BC031922; AAH31922.1; -; mRNA.
DR   CCDS; CCDS26205.1; -.
DR   RefSeq; NP_031789.1; NM_007763.3.
DR   AlphaFoldDB; P63254; -.
DR   SMR; P63254; -.
DR   BioGRID; 198885; 1.
DR   STRING; 10090.ENSMUSP00000006523; -.
DR   iPTMnet; P63254; -.
DR   PhosphoSitePlus; P63254; -.
DR   CPTAC; non-CPTAC-3355; -.
DR   EPD; P63254; -.
DR   jPOST; P63254; -.
DR   MaxQB; P63254; -.
DR   PaxDb; P63254; -.
DR   PeptideAtlas; P63254; -.
DR   PRIDE; P63254; -.
DR   ProteomicsDB; 285332; -.
DR   DNASU; 12925; -.
DR   Ensembl; ENSMUST00000006523; ENSMUSP00000006523; ENSMUSG00000006360.
DR   Ensembl; ENSMUST00000200553; ENSMUSP00000143680; ENSMUSG00000006360.
DR   GeneID; 12925; -.
DR   KEGG; mmu:12925; -.
DR   UCSC; uc007pfz.1; mouse.
DR   CTD; 1396; -.
DR   MGI; MGI:88501; Crip1.
DR   VEuPathDB; HostDB:ENSMUSG00000006360; -.
DR   eggNOG; KOG1700; Eukaryota.
DR   GeneTree; ENSGT00940000162342; -.
DR   HOGENOM; CLU_026811_4_1_1; -.
DR   InParanoid; P63254; -.
DR   OrthoDB; 1214165at2759; -.
DR   PhylomeDB; P63254; -.
DR   BioGRID-ORCS; 12925; 2 hits in 70 CRISPR screens.
DR   ChiTaRS; Crip1; mouse.
DR   PRO; PR:P63254; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; P63254; protein.
DR   Bgee; ENSMUSG00000006360; Expressed in small intestine Peyer's patch and 241 other tissues.
DR   ExpressionAtlas; P63254; baseline and differential.
DR   Genevisible; P63254; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071236; P:cellular response to antibiotic; ISS:UniProtKB.
DR   GO; GO:0071493; P:cellular response to UV-B; ISS:UniProtKB.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; ISS:UniProtKB.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00132; LIM; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; LIM domain; Metal-binding; Methylation; Reference proteome;
KW   Zinc.
FT   CHAIN           1..77
FT                   /note="Cysteine-rich protein 1"
FT                   /id="PRO_0000075708"
FT   DOMAIN          2..63
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P50238"
FT   MOD_RES         22
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         68
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
SQ   SEQUENCE   77 AA;  8550 MW;  BBE8E17A19352EC1 CRC64;
     MPKCPKCDKE VYFAERVTSL GKDWHRPCLK CEKCGKTLTS GGHAEHEGKP YCNHPCYSAM
     FGPKGFGRGG AESHTFK
 
 
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