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Database: UniProt
Entry: A0A3Q3ATP5_KRYMA
LinkDB: A0A3Q3ATP5_KRYMA
Original site: A0A3Q3ATP5_KRYMA 
ID   A0A3Q3ATP5_KRYMA        Unreviewed;       325 AA.
AC   A0A3Q3ATP5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Protein CYR61-like {ECO:0000313|Ensembl:ENSKMAP00000014854.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014854.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000014854.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; A0A3Q3ATP5; -.
DR   Ensembl; ENSKMAT00000015072.1; ENSKMAP00000014854.1; ENSKMAG00000011033.1.
DR   GeneTree; ENSGT00940000155151; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000867; IGFBP-like.
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; PF00219; IGFBP; 1.
DR   Pfam; PF19035; TSP1_CCN; 1.
DR   Pfam; PF00093; VWC; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          7..79
FT                   /note="IGFBP N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51323"
FT   DOMAIN          83..149
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   DOMAIN          231..304
FT                   /note="CTCK"
FT                   /evidence="ECO:0000259|PROSITE:PS01225"
FT   REGION          153..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   325 AA;  36302 MW;  2E1D107F880520A1 CRC64;
     MCNNVFAEGE CPSECFCSPS PVQCPPGVSW VTDHCGCCKV CARQFNEDCS ATEPCDHIKG
     LRCHLGAGGN PKRGLCRAEA HGLPCTFNGR VYQHSEDFQP ICQHQCTCMN GVVGCMPVCP
     YQVPLPRQSC TRPRLVKSEG GCCEEWVCDD DDNRISEDPR EQQTDSSQPD SQPHSHPNHI
     STTEWTPCST TCGMGISSRV TNNNTDCQML RETRLCQIQQ CELQPPVGKK CQRTVRPQRA
     VRITFAGCLT VQRFRPHTCG TCTDGRCCTP SVTRTVRLLF RCSDKETFYN VMWIKRCHCS
     RSCHTDVQPS GSSVSLYNDI HTFKD
//
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