CRIM1_MOUSE
ID CRIM1_MOUSE Reviewed; 1037 AA.
AC Q9JLL0; Q497W4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cysteine-rich motor neuron 1 protein;
DE Short=CRIM-1;
DE Flags: Precursor;
GN Name=Crim1;
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-1037, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11084657;
RX DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1072>3.0.co;2-i;
RA Georgas K., Bowles J., Yamada T., Koopman P., Little M.H.;
RT "Characterisation of Crim1 expression in the developing mouse urogenital
RT tract reveals a sexually dimorphic gonadal expression pattern.";
RL Dev. Dyn. 219:582-587(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10842084; DOI=10.1016/s0925-4773(00)00292-6;
RA Lovicu F.J., Kolle G.V., Yamada T., Little M.H., McAvoy J.W.;
RT "Expression of Crim1 during murine ocular development.";
RL Mech. Dev. 94:261-265(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BMP4 and BMP7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed during embryonic development in brain,
CC kidney, spinal chord, testis, lens, vibrissae, pinna, tooth primordia
CC and in specific regions of the CNS. Expressed in adult lens. Displays
CC male-specific expression in the fetal gonads with the strongest
CC expression in the Sertoli cells of developing testis.
CC {ECO:0000269|PubMed:10642437, ECO:0000269|PubMed:10842084,
CC ECO:0000269|PubMed:11084657}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryo at 11.5 dpc to 17.7 dpc with a
CC maximum between 12.5 and 13.5 dpc. {ECO:0000269|PubMed:10642437,
CC ECO:0000269|PubMed:11084657}.
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DR EMBL; BC100348; AAI00349.1; -; mRNA.
DR EMBL; AF168680; AAF34410.1; -; mRNA.
DR CCDS; CCDS28976.1; -.
DR RefSeq; NP_056615.1; NM_015800.3.
DR AlphaFoldDB; Q9JLL0; -.
DR SMR; Q9JLL0; -.
DR STRING; 10090.ENSMUSP00000108117; -.
DR GlyConnect; 2246; 1 N-Linked glycan (1 site).
DR GlyGen; Q9JLL0; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9JLL0; -.
DR PhosphoSitePlus; Q9JLL0; -.
DR EPD; Q9JLL0; -.
DR MaxQB; Q9JLL0; -.
DR PaxDb; Q9JLL0; -.
DR PeptideAtlas; Q9JLL0; -.
DR PRIDE; Q9JLL0; -.
DR ProteomicsDB; 277895; -.
DR Antibodypedia; 617; 175 antibodies from 28 providers.
DR Ensembl; ENSMUST00000112498; ENSMUSP00000108117; ENSMUSG00000024074.
DR GeneID; 50766; -.
DR KEGG; mmu:50766; -.
DR UCSC; uc008dou.2; mouse.
DR CTD; 51232; -.
DR MGI; MGI:1354756; Crim1.
DR VEuPathDB; HostDB:ENSMUSG00000024074; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000160910; -.
DR HOGENOM; CLU_008434_0_0_1; -.
DR InParanoid; Q9JLL0; -.
DR OMA; HSGCRTC; -.
DR OrthoDB; 1223914at2759; -.
DR PhylomeDB; Q9JLL0; -.
DR TreeFam; TF106451; -.
DR BioGRID-ORCS; 50766; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Crim1; mouse.
DR PRO; PR:Q9JLL0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JLL0; protein.
DR Bgee; ENSMUSG00000024074; Expressed in pigmented layer of retina and 270 other tissues.
DR ExpressionAtlas; Q9JLL0; baseline and differential.
DR Genevisible; Q9JLL0; MM.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..1037
FT /note="Cysteine-rich motor neuron 1 protein"
FT /id="PRO_0000021002"
FT TOPO_DOM 35..940
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962..1037
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 1036
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZV1"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1037 AA; 114066 MW; C41948C0A2B66EA3 CRC64;
MYLVAGGRGL AGCGHLSVSL LGLLLLLARS GTRALVCLPC DESKCEEPRS CPGSIVQGVC
GCCYMCARQR NESCGGAYGL HGACDRGLRC VIRPPLNGDS ITEYEVGVCE DEDWDDDQLI
GFEPCNENLI SGCNIINGKC ECGTIRTCNN PFEFPRKDMC LSALKRIEEE KPDCSKARCE
VRFSPRCPED SILIEGYAPP GECCPLPSRC VCDPAGCLRK VCQPGYLNIL VSKASGKPGE
CCDLYECKPV FSVDCSTVEC PPVQQAVCPL DSYETQVRLT ADGCCTLPAR CECLSGLCGF
PVCEVGSTPR IVSRGDGTPG KCCDVFECVN ETKPACVFNS VEYYDGDMFR MDNCRFCRCQ
GGVSICFTAQ CGELNCERYY VPEGECCPVC EDPIYPLNNP AGCYANGQIR AHGDRWREDD
CTFCQCINGE PHCVATACGQ SCMHPVKVPG ECCPVCEEPT YITIDPPACG ELSNCSLKEK
DCVYGFKLDH NGCRTCQCKI REELCLGLKR ACTLDCPFGF LTDVHNCELC QCRPRPKKCR
PTMCDKFCPL GFLKNKHGCD ICRCKKCPEL PCSKICPLGF QQDSHGCLIC KCREVPPSAG
PPVLSGTCLS MDGHHHKNEE SWHDGCRECY CHNGKEMCAL ITCPVPACGN PTIRSGQCCP
SCTDDFVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVLC ETEVCPPLLC
QNPSRTQDSC CPQCTDDPPQ PSTSHNESVP SYCRNDEGDI FLAAESWKPD ACTSCVCVDS
AISCYSESCP SVACERPVLR KGQCCPYCLE DTIPKKVVCH FSGKTYADEE RWDIDSCTHC
YCLQGQTLCS TVSCPPLPCA EPIKVEGSCC PMCPEMYVPE PTNVPIEKKN HRGEIDLEVP
MWPTPSENDI IHLPRDMGHL QVDYRDNNRL HPGEDSSLDS IVSVVVPIII CLSIIIAFLL
INQKKQWVPL LCWYRTPTKP SSLNNQLVSV DCKKGTRVQV DGPQRMLRIA EPDARFSGFY
SMQKQNHLQA DNFYQTV
