ID V9KRJ7_CALMI Unreviewed; 378 AA.
AC V9KRJ7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Protein CYR61-like {ECO:0000313|EMBL:AFP00976.1, ECO:0000313|Ensembl:ENSCMIP00000004109.1};
GN Name=LOC103183076 {ECO:0000313|Ensembl:ENSCMIP00000004109.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP00976.1};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|EMBL:AFP00976.1, ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:AFP00976.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000004109.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JW868458; AFP00976.1; -; mRNA.
DR RefSeq; XP_007898530.1; XM_007900339.1.
DR Ensembl; ENSCMIT00000004265.1; ENSCMIP00000004109.1; ENSCMIG00000002470.1.
DR GeneID; 103183076; -.
DR KEGG; cmk:103183076; -.
DR GeneTree; ENSGT00940000155151; -.
DR OMA; RPCEFNG; -.
DR OrthoDB; 2970572at2759; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
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:SF34; EPIDERMAL CELL SURFACE RECEPTOR-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 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000314986};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..378
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040664386"
FT DOMAIN 18..90
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 94..160
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 283..357
FT /note="CTCK"
FT /evidence="ECO:0000259|PROSITE:PS01225"
FT REGION 165..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 42567 MW; 00119C23BDF01D53 CRC64;
MEAHLCLTLI VLCWLPLVAS SCPAECHCPD APPSCTPGIS LVLDRCNCCK ICARQFNQDC
SPTEPCDHIK GLECNYATSD VTERGICRAK SEGRPCAFNG NIYQNGENFK PNCKHQCTCI
DSVVGCMPLC PQELSLPTMD CLKPQLVKIS GQCCEEWMCD SNHIGEDSGD TTEEADDSMS
YEEIEDQPDA EPLSSNELMD LVRAGINIQP AWRLQAQEQK SDRPRCIVQT TEWSHCSKSC
GIGISTRVTN DNPQCKLMKE TRLCQLRPCG LSTNTNLKKG KKCFRMKRAK EPVHFTYAGC
TSVRSYEPRW CGSCTDGRCC TPSQTRTIHV RFRCDDGETF SKSVMWINKC RCHYNCPHQN
EISYPYYTLH NDIHKFSE
//