Q9NZV1 (CRIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cysteine-rich motor neuron 1 protein
Short name=CRIM-1

Alternative name(s):
Cysteine-rich repeat-containing protein S52

Cleaved into the following chain:

1. Processed cysteine-rich motor neuron 1 protein

Gene names

Name:	CRIM1
Synonyms:	S52
ORF Names:	UNQ1886/PRO4330

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1036 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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. Ref.5 Ref.7
Subunit structure	Interacts with BMP4 and BMP7. Ref.5
Subcellular location	Processed cysteine-rich motor neuron 1 protein: Secreted Ref.5. Cell membrane; Single-pass type I membrane protein Ref.5.
Tissue specificity	Expressed in pancreas, kidney, skeletal muscle, lung, placenta, brain, heart, spleen, liver and small intestine. Expressed in blood vessels (at protein level). Ref.1 Ref.7
Post-translational modification	N-glycosylated. Ref.5 Ref.7
Sequence similarities	Contains 4 antistasin-like domains. Contains 1 IGFBP N-terminal domain. Contains 6 VWFC domains.
Sequence caution	The sequence BAD92376.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of catalytic activity Inferred from electronic annotation. Source: GOC nervous system development Traceable author statement Ref.1. Source: ProtInc regulation of cell growth Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	insulin-like growth factor-activated receptor activity Traceable author statement Ref.1. Source: ProtInc serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 34	34	Ref.5 Ref.6
	Chain	35 – 1036	1002	Cysteine-rich motor neuron 1 protein		PRO_0000021001
	Chain	? – 1036		Processed cysteine-rich motor neuron 1 protein		PRO_0000296243
Regions
	Topological domain	35 – 939	905	Extracellular Potential
	Transmembrane	940 – 960	21	Helical; Potential
	Topological domain	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
Amino acid modifications
	Modified residue	1035	1	Phosphothreonine Ref.8
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	113	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	474	1	N-linked (GlcNAc...) Potential
	Glycosylation	746	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	502	1	E → K. Corresponds to variant rs12997487 [ dbSNP | Ensembl ].		VAR_050907
	Natural variant	781	1	V → I. Corresponds to variant rs59929305 [ dbSNP | Ensembl ].		VAR_061625
Experimental info
	Sequence conflict	433	1	C → F in BAD92376. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NZV1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 10CBF02A5C579C27	FASTA	1,036	113,738
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CRIM1, a novel gene encoding a cysteine-rich repeat protein, is developmentally regulated and implicated in vertebrate CNS development and organogenesis." Kolle G.V., Georgas K., Holmes G.P., Little M.H., Yamada T. Mech. Dev. 90:181-193(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[2]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." 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. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[5]	"CRIM1 regulates the rate of processing and delivery of bone morphogenetic proteins to the cell surface." Wilkinson L., Kolle G.V., Wen D., Piper M., Scott J., Little M.H. J. Biol. Chem. 278:34181-34188(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-44, FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, INTERACTION WITH BMP4 AND BMP7, IDENTIFICATION OF A SOLUBLE FORM.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-49.
[7]	"CRIM1 is involved in endothelial cell capillary formation in vitro and is expressed in blood vessels in vivo." Glienke J., Sturz A., Menrad A., Thierauch K.-H. Mech. Dev. 119:165-175(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, GLYCOSYLATION, TISSUE SPECIFICITY.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF167706 mRNA. Translation: AAF34409.1. AF168681 Genomic DNA. Translation: AAG37011.1. AB209139 mRNA. Translation: BAD92376.1. Different initiation. AY358371 mRNA. Translation: AAQ88737.1. BC111989 mRNA. Translation: AAI11990.1. BC113371 mRNA. Translation: AAI13372.1.
IPI	IPI00009294.
RefSeq	NP_057525.1. NM_016441.2.
UniGene	Hs.699247.
3D structure databases
ProteinModelPortal	Q9NZV1.
SMR	Q9NZV1. Positions 34-95, 332-393, 402-457, 606-667, 682-736, 752-812, 816-880.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-58932N.
IntAct	Q9NZV1. 4 interactions.
STRING	9606.ENSP00000280527.
PTM databases
PhosphoSite	Q9NZV1.
Polymorphism databases
DMDM	67460590.
Proteomic databases
PaxDb	Q9NZV1.
PeptideAtlas	Q9NZV1.
PRIDE	Q9NZV1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000280527; ENSP00000280527; ENSG00000150938. ENST00000574904; ENSP00000459137; ENSG00000261899.
GeneID	51232.
KEGG	hsa:51232.
UCSC	uc002rpd.3. human.
Organism-specific databases
CTD	51232.
GeneCards	GC02P036495.
H-InvDB	HIX0030218.
HGNC	HGNC:2359. CRIM1.
HPA	HPA000556.
MIM	606189. gene.
neXtProt	NX_Q9NZV1.
PharmGKB	PA26877.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG283828.
HOGENOM	HOG000063671.
HOVERGEN	HBG081345.
InParanoid	Q9NZV1.
OMA	RWREDDC.
OrthoDB	EOG4JQ3WR.
PhylomeDB	Q9NZV1.
Gene expression databases
ArrayExpress	Q9NZV1.
Bgee	Q9NZV1.
CleanEx	HS_CRIM1.
Genevestigator	Q9NZV1.
GermOnline	ENSG00000150938. Homo sapiens.
Family and domain databases
Gene3D	2.10.22.10. 3 hits.
InterPro	IPR000867. IGFBP-like. IPR011061. Prot_inh_I14/15_hirudin/antisn. IPR018112. Prot_inh_I15_antistasin. IPR004094. Prot_inh_I15_antistasin-like. IPR001007. VWF_C. [Graphical view]
Pfam	PF02822. Antistasin. 4 hits. PF00093. VWC. 6 hits. [Graphical view]
SMART	SM00121. IB. 1 hit. SM00214. VWC. 6 hits. [Graphical view]
SUPFAM	SSF57262. Antihaemostatic. 3 hits.
PROSITE	PS51252. ANTISTASIN. 4 hits. PS51323. IGFBP_N_2. 1 hit. PS01208. VWFC_1. 6 hits. PS50184. VWFC_2. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CRIM1. human.
GenomeRNAi	51232.
NextBio	54338.
PMAP-CutDB	Q9NZV1.
SOURCE	Search...

Entry information

Entry name

CRIM1_HUMAN

Accession

Primary (citable) accession number: Q9NZV1
Secondary accession number(s): Q2M2G4 , Q59GH0, Q7LCQ5, Q9H318

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.