ID A0A3Q1E9Z4_9TELE Unreviewed; 734 AA.
AC A0A3Q1E9Z4;
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 Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000000716.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000000716.1}
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; A0A3Q1E9Z4; -.
DR STRING; 80966.ENSAPOP00000000716; -.
DR Ensembl; ENSAPOT00000016395.1; ENSAPOP00000000716.1; ENSAPOG00000001950.1.
DR GeneTree; ENSGT00940000154910; -.
DR InParanoid; A0A3Q1E9Z4; -.
DR Proteomes; UP000257200; 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:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1..130
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 125..318
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT REGION 288..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 82219 MW; 8D1E7229F0C7A150 CRC64;
GKSPFKGDKS GPSSMDEGRT LIIEVTADDS ENFFQVWLIF LIKFFFLFGF QIVDEDDTQF
MTNCPPAVTE STPRRRTRIQ VLWTAPPTGS GCVILKASIV QKRIIYFQDE GSLTIRLCEK
ATEAPAIECC ACGTAKYRLT FYGNWSEKVH PKDYPRRANH WSALIGASHS RGYVLWEYGG
YASEGVRQVA EFGSPIKMEE EIRQKGDEVL TVIKTKAQWP AWQPLNLRAA PSAEFSVDRT
RHLMSFLTML GPSPDWNVGL SGEDLCTKDC GWVQRLVTDL IPWDAGTDGG VTYESPNKPT
NPQEKIRPLT SLDHPQSPFY DPEGGAITPV AKVVVERIAR KGEQCNVVPD TIDDIVADIG
QEEKEEDDTP ETCIYSGWSP WSACSSATCE KGRRMRQRML KAQLDLSVPC PHTQDFQPCM
GPGCSMEEPS TCMMSEWISW SACSASCGMG MRSRERYVKQ YPEDGSLCQL NTEETEKCVV
NEECSPSSCV VTEWAEWDPC SVTCGIGMKR RERMVKMPPI DGSMCKTEVA EVEKCMMPEC
HTIPCMLSPW SDWSDCSVTC GRGVRTRQRM LKSDPAECTE ELEQTEKCML PECPVDCMVS
EWSEWSECNK SCGKGHTIRT RMVKLEPQFG GSACPETIQR KKCKIRKCRP KTKEERGGGG
GNRRRRGKQG RDSAVEEQPA GCRMQPWSSW TDCTKHCGGG IQERFMTAKK RAKGSGTAGC
KDRKEIRACN VHPC
//