SPON1_BOVIN
ID SPON1_BOVIN Reviewed; 807 AA.
AC Q9GLX9;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE AltName: Full=Vascular smooth muscle cell growth-promoting factor;
DE Flags: Precursor;
GN Name=SPON1; Synonyms=VSGP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Ovary;
RX PubMed=11368520; DOI=10.1006/abbi.2001.2367;
RA Miyamoto K., Morishita Y., Yamazaki M., Minamino N., Kangawa K., Matsuo H.,
RA Mizutani T., Yamada K., Minegishi T.;
RT "Isolation and characterization of vascular smooth muscle cell growth
RT promoting factor from bovine ovarian follicular fluid and its cDNA cloning
RT from bovine and human ovary.";
RL Arch. Biochem. Biophys. 390:93-100(2001).
CC -!- FUNCTION: Cell adhesion protein that promotes the attachment of spinal
CC cord and sensory neuron cells and the outgrowth of neurites in vitro.
CC May contribute to the growth and guidance of axons in both the spinal
CC cord and the PNS (By similarity). Major factor for vascular smooth
CC muscle cell. {ECO:0000250}.
CC -!- SUBUNIT: Binds to the central extracellular domain of APP and inhibits
CC beta-secretase cleavage of APP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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DR EMBL; AB051389; BAB18460.1; -; mRNA.
DR RefSeq; NP_777168.1; NM_174743.2.
DR AlphaFoldDB; Q9GLX9; -.
DR SMR; Q9GLX9; -.
DR STRING; 9913.ENSBTAP00000012059; -.
DR PaxDb; Q9GLX9; -.
DR PRIDE; Q9GLX9; -.
DR Ensembl; ENSBTAT00000012059; ENSBTAP00000012059; ENSBTAG00000009150.
DR GeneID; 282866; -.
DR KEGG; bta:282866; -.
DR CTD; 10418; -.
DR VEuPathDB; HostDB:ENSBTAG00000009150; -.
DR VGNC; VGNC:35227; SPON1.
DR eggNOG; KOG3539; Eukaryota.
DR GeneTree; ENSGT00940000154910; -.
DR HOGENOM; CLU_014540_1_0_1; -.
DR InParanoid; Q9GLX9; -.
DR OMA; CLRGAGM; -.
DR OrthoDB; 517669at2759; -.
DR TreeFam; TF313353; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000009150; Expressed in theca cell and 106 other tissues.
DR ExpressionAtlas; Q9GLX9; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0050693; F:LBD domain binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.20.100.10; -; 6.
DR Gene3D; 2.60.40.2130; -; 1.
DR Gene3D; 2.60.40.4060; -; 1.
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 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; SSF82895; 6.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT CHAIN 29..807
FT /note="Spondin-1"
FT /id="PRO_0000035864"
FT DOMAIN 29..194
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 195..388
FT /note="Spondin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00364"
FT DOMAIN 442..495
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 501..555
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 558..611
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 614..666
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 668..721
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 754..806
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 156..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 199..336
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 200..340
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 202..415
FT /evidence="ECO:0000250|UniProtKB:Q9HCB6"
FT DISULFID 443..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 454..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 459..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 502..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 513..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 548..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 559..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 570..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 605..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 615..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 626..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 660..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 807 AA; 90976 MW; 4C484B331FB1034C CRC64;
MRLSPVLLRL SRGPALLALA LPLAVALAFS DETLDKVPKS EGYCSRILRV QGTRREGYTE
FSLRVEGDPD FYKPGTSYRV TLSAAPPSYF RGFTLIALKE NREGDKEEDH AGTFQIIDEE
ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PAGTGCVILK ASIVQKRIIY FQDEGSLTKK
LCEQDSTFDG VTDKPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS
KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP AWQPLNVRAA
PSAEFSVDRT RHLMSFLTMM GPSPDWNVGL SAEDLCTKEC GWVQKVVQDL IPWDAGTDSG
VTYESPNKPT IPQEKIRPLT SLDHPQSPFY DPEGGSITQV ARVVIERIAR KGEQCNIVPD
NVDDIVADLA PEEKDEDDTP ETCIYSNWSP WSACSSSTCD KGKRMRQRML KAQLDLSVPC
PDTQDFQPCM GPGCSDEDGS TCTMSEWITW SPCSISCGTG TRSRERYVKQ FPEDGSVCTL
PTEETEKCTV NEECSPSSCL TTEWGEWDEC SATCGMGMKK RHRMVKMSPA DGSMCKAETS
QAEKCMMPEC HTIPCLLSLW SEWSDCSVTC GKGMRTRQRM LKSLAELGDC NEELEQVEKC
MLPECPIDCE LTEWSQWSEC NKSCGKGHMI RTRMIQMEPQ FGGTPCPETV QRKKCRIRKC
LRNPSIQNLR WREARESRRS EQLREESDGD QFPGCRMRPW TAWSECTKLC GGGIQERYMT
VKKRFKSSQF TSCKDKKEIR ACNVHPC
