SPON1_RAT
ID SPON1_RAT Reviewed; 807 AA.
AC P35446;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE Flags: Precursor;
GN Name=Spon1; Synonyms=Sponf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic floor plate;
RX PubMed=1555244; DOI=10.1016/0092-8674(92)90121-r;
RA Klar A., Baldassare M., Jessell T.M.;
RT "F-spondin: a gene expressed at high levels in the floor plate encodes a
RT secreted protein that promotes neural cell adhesion and neurite
RT extension.";
RL Cell 69:95-110(1992).
RN [2]
RP INTERACTION WITH APP.
RX PubMed=14983046; DOI=10.1073/pnas.0308655100;
RA Ho A., Suedhof T.C.;
RT "Binding of F-spondin to amyloid-beta precursor protein: a candidate
RT amyloid-beta precursor protein ligand that modulates amyloid-beta precursor
RT protein cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2548-2553(2004).
RN [3]
RP STRUCTURE BY NMR OF 441-499 AND 613-666, AND DISULFIDE BONDS.
RX PubMed=16736493; DOI=10.1002/prot.21030;
RA Paakkonen K., Tossavainen H., Permi P., Rakkolainen H., Rauvala H.,
RA Raulo E., Kilpelainen I., Guntert P.;
RT "Solution structures of the first and fourth TSR domains of F-spondin.";
RL Proteins 64:665-672(2006).
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.
CC -!- SUBUNIT: Binds to the central extracellular domain of APP and inhibits
CC beta-secretase cleavage of APP.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the floor plate.
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DR EMBL; M88469; AAA41174.1; -; mRNA.
DR PIR; A38152; A38152.
DR RefSeq; NP_742064.1; NM_172067.1.
DR PDB; 1SZL; NMR; -; A=441-499.
DR PDB; 1VEX; NMR; -; A=613-666.
DR PDBsum; 1SZL; -.
DR PDBsum; 1VEX; -.
DR AlphaFoldDB; P35446; -.
DR SMR; P35446; -.
DR IntAct; P35446; 1.
DR STRING; 10116.ENSRNOP00000046944; -.
DR GlyGen; P35446; 2 sites.
DR PaxDb; P35446; -.
DR PRIDE; P35446; -.
DR GeneID; 64456; -.
DR KEGG; rno:64456; -.
DR UCSC; RGD:619918; rat.
DR CTD; 10418; -.
DR RGD; 619918; Spon1.
DR eggNOG; KOG3539; Eukaryota.
DR InParanoid; P35446; -.
DR OrthoDB; 517669at2759; -.
DR PhylomeDB; P35446; -.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR EvolutionaryTrace; P35446; -.
DR PRO; PR:P35446; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0010954; P:positive regulation of protein processing; ISO:RGD.
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 3D-structure; Cell adhesion; Disulfide bond; Extracellular matrix;
KW Glycoprotein; 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_0000035867"
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 ECO:0000269|PubMed:16736493"
FT DISULFID 454..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16736493"
FT DISULFID 459..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16736493"
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 ECO:0000269|PubMed:16736493"
FT DISULFID 626..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16736493"
FT DISULFID 660..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210,
FT ECO:0000269|PubMed:16736493"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1SZL"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:1SZL"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:1SZL"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:1VEX"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:1VEX"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:1VEX"
SQ SEQUENCE 807 AA; 90773 MW; 309525F9EAFEA89A CRC64;
MRLSPAPLRL SRGPALLALA LPLAAALAFS DETLDKVAKS EGYCSRILRA QGTRREGYTE
FSLRVEGDPD FYKPGSSYRV TLSAAPPSYF RGFTLIALKE NREGDKEEDH AGTFQIIDEE
ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PTGTGCVILK ASIVQKRIIY FQDEGSLTKK
LCEQDPTLDG VTDRPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS
KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP SWQPVNVRAA
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 FGGAPCPETV QRKKCRARKC
LRSPSIQKLR WREARESRRS EQLREESDGE QFPGCRMRPW TAWSECTKLC GGGIQERYMT
VKKRFKSSQF TSCKDKKEIR ACNVHPC
