CRIM1_DANRE
ID CRIM1_DANRE Reviewed; 1027 AA.
AC Q7T3Q2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Cysteine-rich motor neuron 1 protein;
DE Short=CRIM-1;
DE Flags: Precursor;
GN Name=crim1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kolle G.V., Little M.;
RT "Characterization of zebrafish crim1 ortholog.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in CNS development by interacting with growth
CC factors implicated in motor neuron differentiation and survival.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AY151045; AAN72833.1; -; mRNA.
DR RefSeq; NP_997986.1; NM_212821.1.
DR AlphaFoldDB; Q7T3Q2; -.
DR SMR; Q7T3Q2; -.
DR STRING; 7955.ENSDARP00000050533; -.
DR PaxDb; Q7T3Q2; -.
DR GeneID; 404210; -.
DR KEGG; dre:404210; -.
DR CTD; 51232; -.
DR ZFIN; ZDB-GENE-040312-2; crim1.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q7T3Q2; -.
DR OrthoDB; 1223914at2759; -.
DR PhylomeDB; Q7T3Q2; -.
DR PRO; PR:Q7T3Q2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR GO; GO:0048570; P:notochord morphogenesis; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
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; 5.
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; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1027
FT /note="Cysteine-rich motor neuron 1 protein"
FT /id="PRO_0000020999"
FT TOPO_DOM 29..931
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 953..1027
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..106
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 328..385
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 395..451
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 463..492
FT /note="Antistasin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 499..526
FT /note="Antistasin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 533..558
FT /note="Antistasin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 561..586
FT /note="Antistasin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 601..658
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 672..730
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 746..804
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 810..867
FT /note="VWFC 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 877..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..310
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 883..885
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 879..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1027 AA; 112223 MW; E831F8CF174344CC CRC64;
MASSRMYLLV KCMLILQLMV LIAKNSRALI CLPCDKSKCE EPKPCTGSVV LGICGCCSVC
AKQKNESCGG VYGLYGTCDR GLRCVIRPPL NGGSITQYEV GNCEDENWDD DQLLGFEPCN
ENLVTGCNII DGKCECDSVR TCNNPFEFAS QEACQTALQK IEEERPDCSK ARCEVQFSPR
CPEDSILIEG YAPPGECCPL PSRCVCSPAG CLRKVCQPGH LNILVSKSSG KPGECCDLYE
CKPVFSVDCS TVECPPVKPV QCPADSYETQ VRLTADGCCT LPTRCECLPG LCTFPQCSAG
MSPQVMSRGD GTPGRCCDVF ECVNETKPAC TLNGVEYHDG DMFRMDACRF CRCQGGVSVC
FTAQCGVLHC ERYYVPDGEC CPVCEDPIYP VLSLAGCYVN GQILAHGDHW REDDCTFCQC
VSGDARCVAA ACGHSCLNPV TVPGECCPVC EEPTYITMAP PACGSLDNCT LLEQSCAFGF
RLDPSGCRTC ACKSREELCG GLMASCTLKC PFGFQTDIHG CDVCQCRPRH KKCKAVACAK
DCPFGYIKNK HGCDTCRCKK CPELPCDKAC PMGFQHDELG CLICQCRDQS SSSVTPAVKL
GSCLSMDGRR HENGQSWHDG CRDCYCHAGR EMCALISCPV PPCDNPTIRP GHCCPTCPEE
SSSHKPELSE ASVCLAPGGE YFVEGETWNI DSCTQCTCHS GRVLCETEVC PPLLCHSPIR
TQDSCCPHCP DDPVTPQTPS NDSMPSYCRN EDGDIFLAAE SWKPNVCSSC VCLDGAISCF
SESCPPVNCA RPVLRKGQCC PYCLDATPRA VCHFNGKTYM DEERWDIDSC THCYCLQGQT
LCSTVSCPAL PCHQPLTVEG SCCPMCPESY APTNVPIEKT DQRGDKSRHQ PAWPTHSEND
VMPQFRGEFG SLQMPYLDGK TPLPSEDAGL HWAWVALPVL MMMLTLAALL LVNQRKQWIP
VPCYRTPNKS TCLNNQLVYV DCQKGTKVQV DSSQRMLRIA DPDSRYSGYY SMQKHNNLQA
DNFYQTA
