CRIM1_CHICK
ID CRIM1_CHICK Reviewed; 1048 AA.
AC Q8AWW5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cysteine-rich motor neuron 1 protein;
DE Short=CRIM-1;
DE Flags: Precursor;
GN Name=CRIM1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12508231; DOI=10.1002/dvdy.10204;
RA Kolle G.V., Jansen A., Yamada T., Little M.H.;
RT "In ovo electroporation of Crim1 in the developing chick spinal cord.";
RL Dev. Dyn. 226:107-111(2003).
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}.
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic stage 20 in the notchcord
CC and weakly in the foor plate and persist until stage 29. Expressed in
CC the motor neuron pool at stage 23. At stage 26 and 29 highly expressed
CC in the ventrolateral neural tube and also in the roof plate.
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DR EMBL; AY098584; AAM28339.1; -; mRNA.
DR RefSeq; NP_989756.1; NM_204425.1.
DR AlphaFoldDB; Q8AWW5; -.
DR SMR; Q8AWW5; -.
DR STRING; 9031.ENSGALP00000037171; -.
DR PaxDb; Q8AWW5; -.
DR GeneID; 395067; -.
DR KEGG; gga:395067; -.
DR CTD; 51232; -.
DR VEuPathDB; HostDB:geneid_395067; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q8AWW5; -.
DR OrthoDB; 1223914at2759; -.
DR PhylomeDB; Q8AWW5; -.
DR PRO; PR:Q8AWW5; -.
DR Proteomes; UP000000539; 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 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; 3.
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..46
FT /evidence="ECO:0000255"
FT CHAIN 47..1048
FT /note="Cysteine-rich motor neuron 1 protein"
FT /id="PRO_0000021000"
FT TOPO_DOM 47..952
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 974..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..124
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 346..403
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 413..469
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 481..510
FT /note="Antistasin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 517..544
FT /note="Antistasin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 551..576
FT /note="Antistasin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 579..604
FT /note="Antistasin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT DOMAIN 618..675
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 689..747
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 763..821
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 829..886
FT /note="VWFC 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT MOTIF 326..328
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 904..906
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1048 AA; 114943 MW; 25E4D82C40B08231 CRC64;
MYLAAVSAGR RRPGGDGGGG GGGWHLAAAG WLLLLALLLG QPGTRALVCL PCDESKCEEP
KSCPGIIVLG ICGCCFMCAR QRNESCGGVY GLHGACDRGL RCVIRPPLNG DSITEYEVGV
CEDENWDDDQ LLGFEPCNEN LITGCNIING KCDCDTIRTC NNPFEFPSRD TCLSALKRIE
EEKPDCSKAR CEVQFSPRCP EDSILIEGYA PPGECCPLPS RCVCNPAGCL RKVCQPGYLN
ILVSKASGKP GECCDLYECK PVFSVDCSTV ECPPVQQVVC PLDSYETQVR LTADGCCTLP
TRCECLSGLC GFPMCEAGSV PQIVSRGDGT PGKCCDVFEC VNEVKPTCIF NSMEYYDGDM
FRMDACRFCR CQGGVSICFS AQCGELHCDR YYVPEGECCP VCEDPVYPVN NPAGCYANGQ
IQAHGDRWRE DDCTFCQCIN GNPHCVATAC GQSCLNPVKV PGECCPVCEE PTYITIGPPT
CELLVNCTLT EKDCIYSFKL DQNGCRICQC KTREELCTGL ISGCSLDCSF GFQTDAHNCE
ICQCRPRPKK CKPIVCDKYC PFGYLKNKHG CEICRCKKCP EMPCGKICPM GFQQNSHGCV
ICKCREATAS LMPPVKTGSC LSMDGRRHEN EESWHDGCRE CYCHNGREMC ALITCPVPNC
GNPTIHPGQC CPSCPDEIIV QKPELTSPSI CHAPGGEYFV EGETWNIDSC TQCTCHSGRV
LCETEVCPPL LCQNPTRTQD SCCPQCPDEP LQPSLSSNVS MPSYCKNDEG DIFLTAESWK
PNVCTSCICM DGVIRCYSES CPPVSCERPV LRKGQCCPYC IEDTVPKKVV CHFNGKTYAD
EERWDIDSCT HCYCLQGQTL CSTVSCPPLP CAEPINVEGS CCPMCPEMYV PEPTNIPIEK
TNHRGDVELE VPNWSTPSEN DIIHIHRDMN HLQGEYRSGN GPHPSEDASV SSVALVTVPI
TIALLVIIVF LLINQKKQWI PVSCYKAPTK PSCLNNQLVY VDCKKGTMVQ VDSSQRMLRI
ADPDSRYSGF YSMQKQNNLQ ADNFYQTV
