ID A0A3Q3X2V2_MOLML Unreviewed; 798 AA.
AC A0A3Q3X2V2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000025203.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000025203.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A3Q3X2V2; -.
DR STRING; 94237.ENSMMOP00000025203; -.
DR Ensembl; ENSMMOT00000025625.1; ENSMMOP00000025203.1; ENSMMOG00000019142.1.
DR OMA; SGCIAIR; -.
DR Proteomes; UP000261620; 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 Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..798
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018745978"
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..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 89760 MW; D69DDC22932444E8 CRC64;
MGVHMHLLLL QYYLVSSLVC NAVAFVEEPS GGRSDPYCGR ILRAQTQGTR RDGHHEFRLR
VEGDPESYQP GSTYRVVLMA TSPAYFRGFT LIALKEGREG TTDDDYTGQF QIIDKVDTQF
MTNCAPAVTE STPRRRTRIQ VFWTAPASGT GCVILKASIV QKKVIYFQDQ GSLTIRLCEK
ERVAGESTET PAMECCACGT AKYRLTFYGN WSEKVHPKDY PRRANHWSAL IGASHSRRYV
LWEYGGYASE GVRQVAEFGS PIKMEEEIRQ KGDEVMTVIK TKAQWPAWQP LNLRAAPSAE
FSVDRTRHLM SFLTMLGPSP DWNVGLSGED LCTKECGWVP RLETDLIPWD AGTDSGVTYE
SPNKPTIPQA KIRPLTSLDH PQSPFYDPEG GAITSIARVV VERIARKGEQ CNVIPDTIDD
IVADIGQEEK EEDDTPETCI YSGWSPWSAC SSATCEKGRR MRQRMLKAQL DLSVPCPHTQ
DFQPCMAPGC SMEGKPTCMM SEWISWSACS VSCGMGMRSR ERYVKQYPED GSLCQLHTEE
REKCVINDEC SPSSCVVTEW GEWDPCSVTC GLGMRRRERM VKMPPIDGSM CKTEVSEVEK
CMMPECHTIP CILSPWSQWS VCSVTCGQGV RTRQRMLKSD PLDCVEELEQ TEKCMLPECP
VDCMVSEWSE WSECNKSCGK GHTIRTRMIK LEPQFGGSPC PETIQRKKCK IRKCRTKAKD
ERGGGGKRRR RGKQGRDAAV EEQQGCRMQP WTGWTDCTKP CGGGIQERFM NAKRRAKGAM
MASCKNRKEI RACNVHPC
//
