ID A0A3B3QSN1_9TELE Unreviewed; 378 AA.
AC A0A3B3QSN1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protein CYR61-like {ECO:0000313|Ensembl:ENSPKIP00000009143.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000009143.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000009143.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000256|ARBA:ARBA00008125}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00039}.
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DR AlphaFoldDB; A0A3B3QSN1; -.
DR Ensembl; ENSPKIT00000033241.1; ENSPKIP00000009143.1; ENSPKIG00000024360.1.
DR GeneTree; ENSGT00940000155151; -.
DR OrthoDB; 2970572at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR012395; IGFBP_CNN.
DR InterPro; IPR043973; TSP1_CCN.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR11348; CONNECTIVE TISSUE GROWTH FACTOR-RELATED; 1.
DR PANTHER; PTHR11348:SF33; ZGC:112060-RELATED; 1.
DR Pfam; PF00007; Cys_knot; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF19035; TSP1_CCN; 1.
DR Pfam; PF00093; VWC; 1.
DR PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR SMART; SM00041; CT; 1.
DR SMART; SM00121; IB; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..378
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017284925"
FT DOMAIN 23..98
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 102..168
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 283..357
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT REGION 173..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41515 MW; A122FFE9CFB10EAB CRC64;
MFAPKSLAPA SLLTLLPLLC ITAATVNSSC PRVCSCLSSP PICPPGVSLA TDACGCCRVC
ARQFNQDCSP SQPCDHIKGL RCQMAANGDP DRGLCRADAQ GRPCEFGGRL YQHGEHFQPS
CQHQCSCMDG VLGCMPLCPH RMPLPDPRCA SPRLQRPEGR CCEEWVCEDS NHVGEGPPGP
PAHPNAINSA LLPPPPDSRH PGAAGTFQEW KSRPRSFVQS LQTAQCLPQT TNWSECSATC
GMGVSSRVTN SNAECQLVRE TRLCQIRPCD PEVRPQLKRG KKCQRTVWPR QPVRITFAGC
STAKWYRPRS CGSCSDSRCC TPSLTRTVRL RFHCPDGESF THRLMWIRRC RCQRHCPTHG
NASGPSISLH NDVHTYAH
//
