SRPX2_RAT
ID SRPX2_RAT Reviewed; 466 AA.
AC B5DF94;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sushi repeat-containing protein SRPX2 {ECO:0000303|PubMed:24179158};
DE Flags: Precursor;
GN Name=Srpx2 {ECO:0000312|EMBL:AAI68975.1, ECO:0000312|RGD:1562444};
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] {ECO:0000312|EMBL:EDM07041.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI68975.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/NHsdMcwi {ECO:0000312|EMBL:AAI68975.1};
RC TISSUE=Embryonic brain {ECO:0000312|EMBL:AAI68975.1};
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 [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF TYR-73.
RX PubMed=24179158; DOI=10.1126/science.1245079;
RA Sia G.M., Clem R.L., Huganir R.L.;
RT "The human language-associated gene SRPX2 regulates synapse formation and
RT vocalization in mice.";
RL Science 342:987-991(2013).
CC -!- FUNCTION: Acts as a ligand for the urokinase plasminogen activator
CC surface receptor. Plays a role in angiogenesis by inducing endothelial
CC cell migration and the formation of vascular network (cords). Involved
CC in cellular migration and adhesion. Increases the phosphorylation
CC levels of FAK. Interacts with and increases the mitogenic activity of
CC HGF (By similarity). Promotes synapse formation.
CC {ECO:0000250|UniProtKB:O60687, ECO:0000250|UniProtKB:Q8R054,
CC ECO:0000269|PubMed:24179158}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with PLAUR (via the UPAR/Ly6
CC domains), ADAMTS4 and CTSB. Interacts with HGF; the interaction
CC increases the mitogenic activity of HGF. {ECO:0000250|UniProtKB:O60687,
CC ECO:0000269|PubMed:24179158}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O60687}.
CC Cytoplasm {ECO:0000250|UniProtKB:O60687}. Cell surface
CC {ECO:0000269|PubMed:24179158}. Synapse {ECO:0000269|PubMed:24179158}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher levels in the cerebral cortex
CC of juveniles than adults (at protein level).
CC {ECO:0000269|PubMed:24179158}.
CC -!- PTM: Contains chondroitin sulfate chains.
CC {ECO:0000250|UniProtKB:O60687}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH473969; EDM07041.1; -; Genomic_DNA.
DR EMBL; BC168975; AAI68975.1; -; mRNA.
DR RefSeq; NP_001101713.1; NM_001108243.2.
DR RefSeq; XP_017457535.1; XM_017602046.1.
DR RefSeq; XP_017457536.1; XM_017602047.1.
DR AlphaFoldDB; B5DF94; -.
DR STRING; 10116.ENSRNOP00000005020; -.
DR PRIDE; B5DF94; -.
DR Ensembl; ENSRNOT00000103433; ENSRNOP00000085502; ENSRNOG00000003715.
DR GeneID; 317181; -.
DR KEGG; rno:317181; -.
DR CTD; 27286; -.
DR RGD; 1562444; Srpx2.
DR eggNOG; ENOG502QREP; Eukaryota.
DR GeneTree; ENSGT00940000159149; -.
DR HOGENOM; CLU_047011_0_0_1; -.
DR OMA; EQRDMCE; -.
DR OrthoDB; 544541at2759; -.
DR PhylomeDB; B5DF94; -.
DR PRO; PR:B5DF94; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000003715; Expressed in lung and 13 other tissues.
DR Genevisible; B5DF94; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR GO; GO:0036458; F:hepatocyte growth factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR CDD; cd00033; CCP; 3.
DR InterPro; IPR025232; DUF4174.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR043555; SRPX-like.
DR InterPro; IPR028768; SRPX2.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR46343; PTHR46343; 1.
DR PANTHER; PTHR46343:SF3; PTHR46343:SF3; 1.
DR Pfam; PF13778; DUF4174; 1.
DR Pfam; PF02494; HYR; 1.
DR Pfam; PF00084; Sushi; 3.
DR SMART; SM00032; CCP; 3.
DR SUPFAM; SSF57535; SSF57535; 3.
DR PROSITE; PS50825; HYR; 1.
DR PROSITE; PS50923; SUSHI; 3.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell adhesion; Cytoplasm; Disulfide bond; Glycoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..466
FT /note="Sushi repeat-containing protein SRPX2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425275"
FT DOMAIN 70..120
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 121..179
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 178..262
FT /note="HYR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 263..322
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 72..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 92..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 123..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 150..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 265..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 293..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT MUTAGEN 73
FT /note="Y->S: Dominant negative; secreted and retains
FT ability to homooligomerize."
FT /evidence="ECO:0000269|PubMed:24179158"
SQ SEQUENCE 466 AA; 52853 MW; C57A54C810850A88 CRC64;
MKTGSLTQRG ALLLLLLLAP AVTPTWYAGS GYSPDESYNE VYAEEVPDTR ALDYRVPRWC
YTLNIQDGEA TCYSPRGGNY HSSLGTRCEL SCDRGFRLIG RKSVQCLPSR RWSGTAYCRQ
MRCHTLPFIT SGTYTCTNGM LLDSRCDYSC SSGYHLEGDR SRICMEDGRW SGGEPVCVDI
DPPKIRCPHS REKIAEPEKL TARVYWDPPL VKDSADGTIT RVTLRGPEPG SHFPEGEHVI
RYTAYDRAYN RASCKFIVKV QVRRCPILKP PQHGYLTCSS AGDNYGAICE YHCDGGYERQ
GTPSRVCQSS RQWSGSPPVC TPMKINVNVN SAAGLLDQFY EKQRLLIVSA PDPSNRYYKM
QISMLQQSTC GLDLRHVTII ELVGQPPQEV GRIREQQLSA GIIEELRQFQ RLTRSYFNMV
LIDKQGIDRE RYMEPVTPEE IFTFIDDYLL SNQELARRAE QRDVCE
