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   27-MAR-2024, entry version 150.
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   GlyCosmos; Q9JLL0; 2 sites, 1 glycan.
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; 10090-ENSMUSP00000108117; -.
DR   PeptideAtlas; Q9JLL0; -.
DR   ProteomicsDB; 277895; -.
DR   Pumba; Q9JLL0; -.
DR   Antibodypedia; 617; 196 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000112498.3; ENSMUSP00000108117.3; ENSMUSG00000024074.9.
DR   GeneID; 50766; -.
DR   KEGG; mmu:50766; -.
DR   UCSC; uc008dou.2; mouse.
DR   AGR; MGI:1354756; -.
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; FNNVEYH; -.
DR   OrthoDB; 2946817at2759; -.
DR   PhylomeDB; Q9JLL0; -.
DR   TreeFam; TF106451; -.
DR   BioGRID-ORCS; 50766; 0 hits in 79 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 272 other cell types or tissues.
DR   ExpressionAtlas; Q9JLL0; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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   Gene3D; 4.10.40.20; -; 1.
DR   Gene3D; 6.20.200.20; -; 6.
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   PANTHER; PTHR46439; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
DR   PANTHER; PTHR46439:SF1; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
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; SSF57603; FnI-like domain; 6.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57262; Leech antihemostatic proteins; 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.
DR   Genevisible; Q9JLL0; MM.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Signal; 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"
FT   DISULFID        37..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        40..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        45..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        74..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT   DISULFID        84..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
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
//