ID A0A3B4VB85_SERDU Unreviewed; 806 AA.
AC A0A3B4VB85;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000028098.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000028098.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A3B4VB85; -.
DR STRING; 41447.ENSSDUP00000028098; -.
DR Ensembl; ENSSDUT00000028589.1; ENSSDUP00000028098.1; ENSSDUG00000020296.1.
DR GeneTree; ENSGT00940000154910; -.
DR OMA; QENENCV; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.60.40.2130; F-spondin domain; 1.
DR Gene3D; 2.60.40.4060; Reeler domain; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 6.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR009465; Spondin_N.
DR InterPro; IPR038678; Spondin_N_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR NCBIfam; NF038123; NF038123_dom; 1.
DR PANTHER; PTHR11311; SPONDIN; 1.
DR PANTHER; PTHR11311:SF16; SPONDIN-1; 1.
DR Pfam; PF02014; Reeler; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 5.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..806
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017473055"
FT DOMAIN 27..193
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 193..386
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT REGION 719..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 90536 MW; DC7CFB934097840E CRC64;
MTPTGLHSRV LLLLCFVSTT ACNTFAFTEE PSERVGKADG YCSRILRAQT NRKDGNNEFR
LRVEGDPDNY QPGSTYRVSV IATSPSYFRG FILIALKEGT EGDKDEDFAG NFQITDEEET
QFMTNCPPAV TESTPRRRTS IRVFWTAPPS GSGCVVLKAS IVQKRIIYFQ DEGSLTKRMC
EKESLYGDAT DKPLLDCCAC GTAKYRVTFY GNWSEKIHPK DYPRRANHWS AIIGSSHSKN
YVLWEYGGFA SDGVKQVAEL GSPVKMEEEI RQKGDDVLTV IKMKAQWPAW QPLNVRAAPS
AEFSVDRTRH LMSFLTMLGP SPDWNVGLSA EDLCTKECGW AQKVVQDLIP WDAGTDSGVT
YESPNKPTMP QDKIRPLTSL DHPQGPFYDP EGGAITPVAR VVVERIARKG EQCNIVPDNV
DDIVADIAQE EKEEDDTPET CIYSNWSPWS ACSSATCEKG KRMRQRMLKA QLDLSVPCPH
TQDFEPCMGP GCSDEDASTC MMSEWITWSP CSLSCGMGTR SRERYVKQFP DDGSVCTLPT
EETENCVVNE ECSPSSCLVT EWGEWDVCSA TCGLGMKRRE RMVKMPPADG SICGAEVLEV
EKCMMPECHT IPCMLSPWSE WSDCSVTCGK GLRTRQRMLK SPVELGECTE ELEQVEKCML
PECPIDCIMS EWTEWSECNK SCGKGHTIRT RMVKLEPQFG GDPCPETIQR KKCKIRKCNR
GQANSDEKKR RKEQREKRRS KQGRAEVASE HPGCKMRPWS SWTECTKLCG GGIQERLMTV
KQRFKTAQLS SCKDRKEIRA CNVHPC
//