ID A0A3Q1GZ56_ANATE Unreviewed; 792 AA.
AC A0A3Q1GZ56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000679.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000000679.2}
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; A0A3Q1GZ56; -.
DR STRING; 64144.ENSATEP00000000679; -.
DR Ensembl; ENSATET00000000693.2; ENSATEP00000000679.2; ENSATEG00000000456.2.
DR GeneTree; ENSGT00940000154910; -.
DR Proteomes; UP000265040; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
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:UP000265040};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..792
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030079280"
FT DOMAIN 34..202
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 202..395
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT REGION 369..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 88885 MW; 3BB4A1CC0869882B CRC64;
MRRFPFSPTP CGLHSRVMLL LCFVSTAACN TFAFTEEPPE RAGKADGYCS RILRAQSNRK
EGTNEFRLRV EGDPESYQPG STYRGWLSVI ASSPSYFRGF TLIALKEGAE GDKDEDYVGN
FQIIDEEEAQ FMTNCPPAVT ESTPRRRTSI QVFWTAPPSG SGCVVLKASI VQKRIIYFQD
EGSLTKRMCE KESLYGDATD KPLLDCCACG TAKYRVTFYG NWSEKIHPKD YPRRANHWSA
IIGASHSKNY VLWEYGGFAS EGVKQVAELG SPVKMEEEIR QKGDEVLTVI KMKAQWPAWQ
PLNVRAAPSA EFSVDRTRHL MSFLTMLGPS PDWNVGLSAE DLCTKECGWA QKVVQDLIPW
DAGTDSGVTY ESPNKPTAPQ EKIRPLTSLD HPQSPFYDPE GGAITPVARV VVERIARKGE
QCNIVPDNVD DIVADIAQEE KEEDDTPETC IYSNWSPWSA CSSATCEKGK RMRQRMLKAQ
LDLSVPCPHT QDFEPCMGPG CSDEDASTCM MSEWITWSPC SMSCGMGTRS RERYVKQFPD
DGSVCTLPTE ETENCVVNED CSPSSCLVTE WGEWDACSAT CGLGMKRRER MVKMPPADGS
ICGAEVLEVE KCMMPECHTI PCLLTPWSDW SDCSVTCGKG LRTRQRVLKS PVELGECSEE
LEQVEKCMLP ECPIDCAMSE WTEWSECNKS CGKGHTIRTR MVKLEPQFGG DPCPESIQRK
KCKIRKCSRR HEKKSSKDRC KMRPWSNWTE CTKLCGGGIQ ERLMTVKRRF KTAQLSSCKD
RKEIRACNVH PC
//