ID A0A3B4TI53_SERDU Unreviewed; 804 AA.
AC A0A3B4TI53;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSSDUP00000005713.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000005713.1}
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; A0A3B4TI53; -.
DR STRING; 41447.ENSSDUP00000005713; -.
DR Ensembl; ENSSDUT00000005826.1; ENSSDUP00000005713.1; ENSSDUG00000004189.1.
DR GeneTree; ENSGT00940000154910; -.
DR OMA; SGCIAIR; -.
DR OrthoDB; 5404502at2759; -.
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..804
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017292357"
FT DOMAIN 23..191
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 191..384
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT REGION 718..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 90073 MW; 82B4FBCD1CDC96CF CRC64;
MGMYLHLLLL QYYFVTSFVC NAVAFVEEPS GGRSDGYCGR ILRAPTHGTR KDGHHEFRLR
VEGDPETYQP GRTYRVVLLA TSPAYFRGFT LIALKEGREG TTDDDYAGQF QIIDEEDTQF
MTNCPPAVTE STPRRRTRIQ VFWTAPPTGT GCVILKASIV QKKIIYFQEE GSLTIRLCEK
ERVFGEATGA PALECCACGT AKYRLTFYGN WSEKVHPKDY PRRANHWSAL IGASHSRGYV
LWEYGGYASE GVRQVAEFGS PIKMEEEIRQ KGDEVLTVIK TKAQWPAWQP LNLRAAPSAE
FSVDRTRHLM SFLTMLGPSP DWNVGLSGED LCTKECGWVQ RLVTDLIPWD AGTDGGVTYE
SPNKPTIPQE KIRPLTSLDH PQSPFYDPEG GAITPVARLV VERIARKGEQ CNVVPDTIDD
IVADIGQEEK EEDDTPETCI YSGWSPWSAC SSATCEKGRR MRQRMLKAQL DLSVPCPHTQ
DFQPCMGPGC SMEEPSTCMM SEWISWSACS VSCGMGMRSR ERYVKQYPED GSLCQLHTEE
TEKCVVNDEC SPSSCVVTEW GEWDPCSVTC GMGMRRRERM VKMPPIDGSM CKTEVAEVEK
CMMPECHTIP CMLSPWSDWS ECSVTCGRGV RTRQRMLKSD PAECSEELEQ TEKCMLPECP
VDCMVSEWSE WSECNKSCGK GHTIRTRMVK LEPQFGGSTC PETIQRKKCK IRKCRTKTKE
ERGGGGGGGG GKRRRRGKQG RDAALEEQPA GCRMQPWSSW TDCTKPCGGG IQERFMMVKK
RAKGALAAGC KDRKEIRACN VHPC
//