CRIM1_HUMAN
ID CRIM1_HUMAN Reviewed; 1036 AA.
AC Q9NZV1; Q2M2G4; Q59GH0; Q7LCQ5; Q9H318;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cysteine-rich motor neuron 1 protein;
DE Short=CRIM-1;
DE AltName: Full=Cysteine-rich repeat-containing protein S52;
DE Contains:
DE RecName: Full=Processed cysteine-rich motor neuron 1 protein;
DE Flags: Precursor;
GN Name=CRIM1; Synonyms=S52; ORFNames=UNQ1886/PRO4330;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10642437; DOI=10.1016/s0925-4773(99)00248-8;
RA Kolle G.V., Georgas K., Holmes G.P., Little M.H., Yamada T.;
RT "CRIM1, a novel gene encoding a cysteine-rich repeat protein, is
RT developmentally regulated and implicated in vertebrate CNS development and
RT organogenesis.";
RL Mech. Dev. 90:181-193(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 35-44, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP INTERACTION WITH BMP4 AND BMP7, AND IDENTIFICATION OF A SOLUBLE FORM.
RX PubMed=12805376; DOI=10.1074/jbc.m301247200;
RA Wilkinson L., Kolle G.V., Wen D., Piper M., Scott J., Little M.H.;
RT "CRIM1 regulates the rate of processing and delivery of bone morphogenetic
RT proteins to the cell surface.";
RL J. Biol. Chem. 278:34181-34188(2003).
RN [6]
RP PROTEIN SEQUENCE OF 35-49.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP FUNCTION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=12464430; DOI=10.1016/s0925-4773(02)00355-6;
RA Glienke J., Sturz A., Menrad A., Thierauch K.-H.;
RT "CRIM1 is involved in endothelial cell capillary formation in vitro and is
RT expressed in blood vessels in vivo.";
RL Mech. Dev. 119:165-175(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May play a role in CNS development by interacting with growth
CC factors implicated in motor neuron differentiation and survival. May
CC play a role in capillary formation and maintenance during angiogenesis.
CC Modulates BMP activity by affecting its processing and delivery to the
CC cell surface. {ECO:0000269|PubMed:12464430,
CC ECO:0000269|PubMed:12805376}.
CC -!- SUBUNIT: Interacts with BMP4 and BMP7. {ECO:0000269|PubMed:12805376}.
CC -!- SUBCELLULAR LOCATION: [Processed cysteine-rich motor neuron 1 protein]:
CC Secreted.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12805376};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12805376}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle,
CC lung, placenta, brain, heart, spleen, liver and small intestine.
CC Expressed in blood vessels (at protein level).
CC {ECO:0000269|PubMed:10642437, ECO:0000269|PubMed:12464430}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12464430,
CC ECO:0000269|PubMed:12805376}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF167706; AAF34409.1; -; mRNA.
DR EMBL; AF168681; AAG37011.1; -; Genomic_DNA.
DR EMBL; AB209139; BAD92376.1; ALT_INIT; mRNA.
DR EMBL; AY358371; AAQ88737.1; -; mRNA.
DR EMBL; BC111989; AAI11990.1; -; mRNA.
DR EMBL; BC113371; AAI13372.1; -; mRNA.
DR CCDS; CCDS1783.1; -.
DR RefSeq; NP_057525.1; NM_016441.2.
DR AlphaFoldDB; Q9NZV1; -.
DR SMR; Q9NZV1; -.
DR BioGRID; 119395; 26.
DR DIP; DIP-58932N; -.
DR IntAct; Q9NZV1; 13.
DR MINT; Q9NZV1; -.
DR STRING; 9606.ENSP00000280527; -.
DR GlyGen; Q9NZV1; 7 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9NZV1; -.
DR PhosphoSitePlus; Q9NZV1; -.
DR SwissPalm; Q9NZV1; -.
DR BioMuta; CRIM1; -.
DR DMDM; 67460590; -.
DR EPD; Q9NZV1; -.
DR jPOST; Q9NZV1; -.
DR MassIVE; Q9NZV1; -.
DR MaxQB; Q9NZV1; -.
DR PaxDb; Q9NZV1; -.
DR PeptideAtlas; Q9NZV1; -.
DR PRIDE; Q9NZV1; -.
DR ProteomicsDB; 83516; -.
DR Antibodypedia; 617; 175 antibodies from 28 providers.
DR DNASU; 51232; -.
DR Ensembl; ENST00000280527.7; ENSP00000280527.2; ENSG00000150938.10.
DR GeneID; 51232; -.
DR KEGG; hsa:51232; -.
DR MANE-Select; ENST00000280527.7; ENSP00000280527.2; NM_016441.3; NP_057525.1.
DR UCSC; uc002rpd.4; human.
DR CTD; 51232; -.
DR DisGeNET; 51232; -.
DR GeneCards; CRIM1; -.
DR HGNC; HGNC:2359; CRIM1.
DR HPA; ENSG00000150938; Tissue enhanced (placenta).
DR MalaCards; CRIM1; -.
DR MIM; 606189; gene.
DR neXtProt; NX_Q9NZV1; -.
DR OpenTargets; ENSG00000150938; -.
DR Orphanet; 468672; Colobomatous macrophthalmia-microcornea syndrome.
DR PharmGKB; PA26877; -.
DR VEuPathDB; HostDB:ENSG00000150938; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000160910; -.
DR HOGENOM; CLU_008434_0_0_1; -.
DR InParanoid; Q9NZV1; -.
DR OMA; HSGCRTC; -.
DR OrthoDB; 1223914at2759; -.
DR PhylomeDB; Q9NZV1; -.
DR TreeFam; TF106451; -.
DR PathwayCommons; Q9NZV1; -.
DR SignaLink; Q9NZV1; -.
DR BioGRID-ORCS; 51232; 4 hits in 1062 CRISPR screens.
DR ChiTaRS; CRIM1; human.
DR GeneWiki; CRIM1; -.
DR GenomeRNAi; 51232; -.
DR Pharos; Q9NZV1; Tbio.
DR PRO; PR:Q9NZV1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NZV1; protein.
DR Bgee; ENSG00000150938; Expressed in saphenous vein and 207 other tissues.
DR ExpressionAtlas; Q9NZV1; baseline and differential.
DR Genevisible; Q9NZV1; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005010; F:insulin-like growth factor receptor activity; TAS:ProtInc.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:ARUK-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR045813; CRIM1_C.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011061; Hirudin/antistatin.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF02822; Antistasin; 4.
DR Pfam; PF19442; CRIM1_C; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00093; VWC; 6.
DR SMART; SM00121; IB; 1.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 4.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57262; SSF57262; 3.
DR PROSITE; PS51252; ANTISTASIN; 4.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS01208; VWFC_1; 6.
DR PROSITE; PS50184; VWFC_2; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:12805376,
FT ECO:0000269|PubMed:15340161"
FT CHAIN 35..1036
FT /note="Cysteine-rich motor neuron 1 protein"
FT /id="PRO_0000021001"
FT CHAIN ?..1036
FT /note="Processed cysteine-rich motor neuron 1 protein"
FT /id="PRO_0000296243"
FT TOPO_DOM 35..939
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 961..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..112
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 334..391
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 401..457
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 469..498
FT /note="Antistasin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 505..532
FT /note="Antistasin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 539..564
FT /note="Antistasin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 567..592
FT /note="Antistasin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 606..663
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 677..735
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 751..809
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 817..874
FT /note="VWFC 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT MOTIF 314..316
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 1035
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 502
FT /note="E -> K (in dbSNP:rs12997487)"
FT /id="VAR_050907"
FT VARIANT 781
FT /note="V -> I (in dbSNP:rs59929305)"
FT /id="VAR_061625"
FT CONFLICT 433
FT /note="C -> F (in Ref. 2; BAD92376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 113738 MW; 10CBF02A5C579C27 CRC64;
MYLVAGDRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN CPGSIVQGVC
GCCYTCASQR NESCGGTFGI YGTCDRGLRC VIRPPLNGDS LTEYEAGVCE DENWTDDQLL
GFKPCNENLI AGCNIINGKC ECNTIRTCSN PFEFPSQDMC LSALKRIEEE KPDCSKARCE
VQFSPRCPED SVLIEGYAPP GECCPLPSRC VCNPAGCLRK VCQPGNLNIL VSKASGKPGE
CCDLYECKPV FGVDCRTVEC PPVQQTACPP DSYETQVRLT ADGCCTLPTR CECLSGLCGF
PVCEVGSTPR IVSRGDGTPG KCCDVFECVN DTKPACVFNN VEYYDGDMFR MDNCRFCRCQ
GGVAICFTAQ CGEINCERYY VPEGECCPVC EDPVYPFNNP AGCYANGLIL AHGDRWREDD
CTFCQCVNGE RHCVATVCGQ TCTNPVKVPG ECCPVCEEPT IITVDPPACG ELSNCTLTGK
DCINGFKRDH NGCRTCQCIN TEELCSERKQ GCTLNCPFGF LTDAQNCEIC ECRPRPKKCR
PIICDKYCPL GLLKNKHGCD ICRCKKCPEL SCSKICPLGF QQDSHGCLIC KCREASASAG
PPILSGTCLT VDGHHHKNEE SWHDGCRECY CLNGREMCAL ITCPVPACGN PTIHPGQCCP
SCADDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVLC ETEVCPPLLC
QNPSRTQDSC CPQCTDQPFR PSLSRNNSVP NYCKNDEGDI FLAAESWKPD VCTSCICIDS
VISCFSESCP SVSCERPVLR KGQCCPYCIE DTIPKKVVCH FSGKAYADEE RWDLDSCTHC
YCLQGQTLCS TVSCPPLPCV EPINVEGSCC PMCPEMYVPE PTNIPIEKTN HRGEVDLEVP
LWPTPSENDI VHLPRDMGHL QVDYRDNRLH PSEDSSLDSI ASVVVPIIIC LSIIIAFLFI
NQKKQWIPLL CWYRTPTKPS SLNNQLVSVD CKKGTRVQVD SSQRMLRIAE PDARFSGFYS
MQKQNHLQAD NFYQTV
