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UniProtKB/Swiss-Prot entry Q9NZV1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CRIM1_HUMAN
Primary accession number Q9NZV1
Secondary accession numbers Q2M2G4 Q59GH0 Q7LCQ5 Q9H318
Integrated into Swiss-Prot on June 7, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name Cysteine-rich motor neuron 1 protein [Precursor]
Synonyms CRIM-1
Cysteine-rich repeat-containing protein S52
Contains Processed cysteine-rich motor neuron 1 protein
Gene name
Name: CRIM1
Synonyms: S52
ORFNames: UNQ1886/PRO4330
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
DOI=10.1016/S0925-4773(99)00248-8; PubMed=10642437 [NCBI, ExPASy, EBI, Israel, Japan]
Kolle G.V., Georgas K., Holmes G.P., Little M.H., Yamada T.;
"CRIM1, a novel gene encoding a cysteine-rich repeat protein, is developmentally regulated and implicated in vertebrate CNS development and organogenesis.";
Mech. Dev. 90:181-193(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 35-44, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, INTERACTION WITH BMP4 AND BMP7, AND IDENTIFICATION OF A SOLUBLE FORM.
DOI=10.1074/jbc.M301247200; PubMed=12805376 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson L., Kolle G.V., Wen D., Piper M., Scott J., Little M.H.;
"CRIM1 regulates the rate of processing and delivery of bone morphogenetic proteins to the cell surface.";
J. Biol. Chem. 278:34181-34188(2003).
[6]
PROTEIN SEQUENCE OF 35-49.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
FUNCTION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0925-4773(02)00355-6; PubMed=12464430 [NCBI, ExPASy, EBI, Israel, Japan]
Glienke J., Sturz A., Menrad A., Thierauch K.-H.;
"CRIM1 is involved in endothelial cell capillary formation in vitro and is expressed in blood vessels in vivo.";
Mech. Dev. 119:165-175(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface.
  • SUBUNIT: Interacts with BMP4 and BMP7.
  • SUBCELLULAR LOCATION: Processed cysteine-rich motor neuron 1 protein: Secreted.
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Expressed in pancreas, kidney, skeletal muscle, lung, placenta, brain, heart, spleen, liver and small intestine. Expressed in blood vessels (at protein level).
  • PTM: N-glycosylated.
  • SIMILARITY: Contains 4 antistasin-like domains.
  • SIMILARITY: Contains 1 IGFBP N-terminal domain.
  • SIMILARITY: Contains 6 VWFC domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF167706; AAF34409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF168681; AAG37011.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209139; BAD92376.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358371; AAQ88737.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111989; AAI11990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113371; AAI13372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057525.1; -.
UniGene Hs.699247
3D structure databases
HSSP P15358; 1SKZ. [HSSP ENTRY / PDB]
ModBase Q9NZV1.
PTM databases
PhosphoSite Q9NZV1; -.
Organism-specific databases
H-InvDB HIX0001964; -.
HIX0030218; -.
HGNC HGNC:2359; CRIM1.
GenAtlas CRIM1.
HPA HPA000556; -.
MIM 606189; gene. [NCBI / EBI]
PharmGKB PA26877; -.
GeneCards Q9NZV1.
Gene expression databases
ArrayExpress Q9NZV1; -.
CleanEx HS_CRIM1; -.
GermOnline ENSG00000150938; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0016021; Cellular component: integral to membrane (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005520; Molecular function: insulin-like growth factor binding (inferred from electronic annotation from InterPro).
GO:0005010; Molecular function: insulin-like growth factor receptor activity (traceable author statement from ProtInc).
GO:0004867; Molecular function: serine-type endopeptidase inhibitor activity (inferred from electronic annotation from InterPro).
GO:0007399; Biological process: nervous system development (traceable author statement from ProtInc).
GO:0001558; Biological process: regulation of cell growth (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000867; IGFBP_like.
IPR004094; Prot_inh_antistn.
IPR001007; VWF_C.
Graphical view of domain structure.
Pfam PF02822; Antistasin; 4.
PF00093; VWC; 6.
Pfam graphical view of domain structure.
SMART SM00121; IB; 1.
SM00214; VWC; 6.
SMART graphical view of domain structure.
PROSITE PS51252; ANTISTASIN; 4.
PS51323; IGFBP_N_2; 1.
PS01208; VWFC_1; 6.
PS50184; VWFC_2; 6.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NZV1.
Proteomic databases
PeptideAtlas Q9NZV1; -.
Genome annotation databases
Ensembl ENSG00000150938; Homo sapiens. [Contig view]
GeneID 51232; -.
KEGG hsa:51232; -.
Phylogenomic databases
HOGENOM Q9NZV1; -.
HOVERGEN Q9NZV1; -.
Other
NextBio 54338; -.
SOURCE CRIM1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; Repeat; Secreted; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     34  34      
CHAIN   35   1036  1002     Cysteine-rich motor neuron 1 protein. PRO_0000021001
CHAIN   ?   1036        Processed cysteine-rich motor neuron 1 protein. PRO_0000296243
TOPO_DOM   35    939  905     Extracellular (Potential). 
TRANSMEM   940    960  21     Potential. 
TOPO_DOM   961   1036  76     Cytoplasmic (Potential). 
DOMAIN   35    112  78     IGFBP N-terminal. 
DOMAIN   334    391  58     VWFC 1. 
DOMAIN   401    457  57     VWFC 2. 
DOMAIN   469    498  30     Antistasin-like 1. 
DOMAIN   505    532  28     Antistasin-like 2. 
DOMAIN   539    564  26     Antistasin-like 3. 
DOMAIN   567    592  26     Antistasin-like 4. 
DOMAIN   606    663  58     VWFC 3. 
DOMAIN   677    735  59     VWFC 4. 
DOMAIN   751    809  59     VWFC 5. 
DOMAIN   817    874  58     VWFC 6. 
MOTIF   314    316  3     Cell attachment site (Potential). 
MOD_RES   1035   1035        Phosphothreonine. 
CARBOHYD   71     71        N-linked (GlcNAc...) (Potential). 
CARBOHYD   113    113        N-linked (GlcNAc...) (Potential). 
CARBOHYD   330    330        N-linked (GlcNAc...) (Potential). 
CARBOHYD   474    474        N-linked (GlcNAc...) (Potential). 
CARBOHYD   746    746        N-linked (GlcNAc...) (Potential). 
CONFLICT   433    433        C -> F (in Ref. 2; BAD92376). 
Sequence information
Length: 1036 AA [This is the length of the unprocessed precursor] Molecular weight: 113738 Da [This is the MW of the unprocessed precursor] CRC64: 10CBF02A5C579C27 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MYLVAGDRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN CPGSIVQGVC 

        70         80         90        100        110        120 
GCCYTCASQR NESCGGTFGI YGTCDRGLRC VIRPPLNGDS LTEYEAGVCE DENWTDDQLL 

       130        140        150        160        170        180 
GFKPCNENLI AGCNIINGKC ECNTIRTCSN PFEFPSQDMC LSALKRIEEE KPDCSKARCE 

       190        200        210        220        230        240 
VQFSPRCPED SVLIEGYAPP GECCPLPSRC VCNPAGCLRK VCQPGNLNIL VSKASGKPGE 

       250        260        270        280        290        300 
CCDLYECKPV FGVDCRTVEC PPVQQTACPP DSYETQVRLT ADGCCTLPTR CECLSGLCGF 

       310        320        330        340        350        360 
PVCEVGSTPR IVSRGDGTPG KCCDVFECVN DTKPACVFNN VEYYDGDMFR MDNCRFCRCQ 

       370        380        390        400        410        420 
GGVAICFTAQ CGEINCERYY VPEGECCPVC EDPVYPFNNP AGCYANGLIL AHGDRWREDD 

       430        440        450        460        470        480 
CTFCQCVNGE RHCVATVCGQ TCTNPVKVPG ECCPVCEEPT IITVDPPACG ELSNCTLTGK 

       490        500        510        520        530        540 
DCINGFKRDH NGCRTCQCIN TEELCSERKQ GCTLNCPFGF LTDAQNCEIC ECRPRPKKCR 

       550        560        570        580        590        600 
PIICDKYCPL GLLKNKHGCD ICRCKKCPEL SCSKICPLGF QQDSHGCLIC KCREASASAG 

       610        620        630        640        650        660 
PPILSGTCLT VDGHHHKNEE SWHDGCRECY CLNGREMCAL ITCPVPACGN PTIHPGQCCP 

       670        680        690        700        710        720 
SCADDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVLC ETEVCPPLLC 

       730        740        750        760        770        780 
QNPSRTQDSC CPQCTDQPFR PSLSRNNSVP NYCKNDEGDI FLAAESWKPD VCTSCICIDS 

       790        800        810        820        830        840 
VISCFSESCP SVSCERPVLR KGQCCPYCIE DTIPKKVVCH FSGKAYADEE RWDLDSCTHC 

       850        860        870        880        890        900 
YCLQGQTLCS TVSCPPLPCV EPINVEGSCC PMCPEMYVPE PTNIPIEKTN HRGEVDLEVP 

       910        920        930        940        950        960 
LWPTPSENDI VHLPRDMGHL QVDYRDNRLH PSEDSSLDSI ASVVVPIIIC LSIIIAFLFI 

       970        980        990       1000       1010       1020 
NQKKQWIPLL CWYRTPTKPS SLNNQLVSVD CKKGTRVQVD SSQRMLRIAE PDARFSGFYS 

      1030 
MQKQNHLQAD NFYQTV 

Q9NZV1 in FASTA format

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