ID SPON1_MOUSE Reviewed; 807 AA.
AC Q8VCC9; Q8K2Q8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE Flags: Precursor;
GN Name=Spon1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC020531; AAH20531.1; -; mRNA.
DR EMBL; BC030339; AAH30339.1; ALT_INIT; mRNA.
DR CCDS; CCDS21757.1; -.
DR RefSeq; NP_663559.1; NM_145584.2.
DR AlphaFoldDB; Q8VCC9; -.
DR SMR; Q8VCC9; -.
DR BioGRID; 231439; 2.
DR IntAct; Q8VCC9; 2.
DR STRING; 10090.ENSMUSP00000041157; -.
DR GlyConnect; 2739; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q8VCC9; 2 sites, 1 glycan.
DR GlyGen; Q8VCC9; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8VCC9; -.
DR PhosphoSitePlus; Q8VCC9; -.
DR SwissPalm; Q8VCC9; -.
DR MaxQB; Q8VCC9; -.
DR PaxDb; 10090-ENSMUSP00000041157; -.
DR ProteomicsDB; 261574; -.
DR Antibodypedia; 62004; 178 antibodies from 26 providers.
DR DNASU; 233744; -.
DR Ensembl; ENSMUST00000046687.16; ENSMUSP00000041157.10; ENSMUSG00000038156.17.
DR GeneID; 233744; -.
DR KEGG; mmu:233744; -.
DR UCSC; uc009jhv.2; mouse.
DR AGR; MGI:2385287; -.
DR CTD; 10418; -.
DR MGI; MGI:2385287; Spon1.
DR VEuPathDB; HostDB:ENSMUSG00000038156; -.
DR eggNOG; KOG3539; Eukaryota.
DR GeneTree; ENSGT00940000154910; -.
DR HOGENOM; CLU_014540_1_0_1; -.
DR InParanoid; Q8VCC9; -.
DR OMA; MMPPKEG; -.
DR OrthoDB; 5404502at2759; -.
DR PhylomeDB; Q8VCC9; -.
DR TreeFam; TF313353; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 233744; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Spon1; mouse.
DR PRO; PR:Q8VCC9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VCC9; Protein.
DR Bgee; ENSMUSG00000038156; Expressed in epithelium of lens and 232 other cell types or tissues.
DR ExpressionAtlas; Q8VCC9; baseline and differential.
DR Genevisible; Q8VCC9; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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; IPI:MGI.
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; IDA:MGI.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; IDA:MGI.
DR GO; GO:0010954; P:positive regulation of protein processing; IDA:MGI.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
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 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..807
FT /note="Spondin-1"
FT /id="PRO_0000035866"
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 REGION 732..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 90821 MW; 3116DF867F4AE563 CRC64;
MRLSPVSLRL SRGPALLALA LPLAAALAFS DETLDKVTKS EGYCSRILRA QGTRREGYTE
FSLRVEGDPD FYKPGSSYRV TLSAAPPSYF RGFTLIALKE NQEGDKEEDH AGTFQIIDEE
ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PTGTGCVILK ASIVQKRIIY FQDEGSLTKK
LCEQDPTLDG VTDRPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS
KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP AWQPVNVRAA
PSAEFSVDRT RHLMSFLTMM GPSPDWNVGL SAEDLCTKEC GWVQKVVQDL IPWDAGTDSG
VTYESPNKPT IPQEKIRPLT SLDHPQSPFY DPEGGSITQV ARVVIERIAR KGEQCNIVPD
NVDDIVADLA PEEKDEDDTP ETCIYSNWSP WSACSSSTCE KGKRMRQRML KAQLDLSVPC
PDTQDFQPCM GPGCSDEDGS TCTMSEWITW SPCSVSCGMG MRSRERYVKQ FPEDGSVCML
PTEETEKCTV NEECSPSSCL VTEWGEWDDC SATCGMGMKK RHRMVKMSPA DGSMCKAETS
QAEKCMMPEC HTIPCLLSPW SEWSDCSVTC GKGMRTRQRM LKSLAELGDC NEDLEQAEKC
MLPECPIDCE LSEWSQWSEC NKSCGKGHMI RTRTIQMEPQ FGGVPCPETV QRKKCRTRKC
LRSPSVQKLR WREARESRRS EQLREESDGE QFPGCRMRPW TAWSECTKLC GGGIQERYMT
VKKRFKSSQF TSCKDKKEIR ACNVHPC
//
