SRPX2_BOVIN
ID SRPX2_BOVIN Reviewed; 465 AA.
AC Q5EA25;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Sushi repeat-containing protein SRPX2;
DE Flags: Precursor;
GN Name=SRPX2;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. Promotes synapse formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts with PLAUR (via
CC the UPAR/Ly6 domains), ADAMTS4 and CTSB. Interacts with HGF; the
CC interaction increases the mitogenic activity of HGF (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell surface {ECO:0000250}. Synapse {ECO:0000250}.
CC -!- PTM: Contains chondroitin sulfate chains. {ECO:0000250}.
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; BT020744; AAX08761.1; -; mRNA.
DR RefSeq; NP_001014926.1; NM_001014926.1.
DR AlphaFoldDB; Q5EA25; -.
DR STRING; 9913.ENSBTAP00000049519; -.
DR PaxDb; Q5EA25; -.
DR PRIDE; Q5EA25; -.
DR GeneID; 514742; -.
DR KEGG; bta:514742; -.
DR CTD; 27286; -.
DR eggNOG; ENOG502QREP; Eukaryota.
DR InParanoid; Q5EA25; -.
DR OrthoDB; 544541at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Angiogenesis; Cell adhesion; Cytoplasm; Disulfide bond; Glycoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi; Synapse.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..465
FT /note="Sushi repeat-containing protein SRPX2"
FT /id="PRO_0000274524"
FT DOMAIN 69..119
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 120..178
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 177..261
FT /note="HYR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 262..321
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 71..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 91..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 122..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 149..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 264..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 292..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 465 AA; 53068 MW; 4CD0FAEAF1B4EBEB CRC64;
MAIQLTRRGA LSLLLFLTPA VMPTWYAGSG YYPDESYNEV YAEEVPQTPI LDYKVPRWCY
TLNIQDGEAT CYSPRGGNYH SSLGTRCELS CDRGFRLIGR RSVQCLPSRR WSGTAYCRQM
RCHALPFITS GTYTCTNGVL LDSRCDYSCS SGYHLEGDRS RICMEDGRWS GGEPVCVDID
PPKIRCPHSR EKMAEPEKLT ARVYWDPPVV KDSADGTITR LTLRGPEPGS HFPEGEHVIR
YTAYDRAYNR ASCKFIVKVQ VRRCPTLKPP LHGYLTCTSA GDNYGATCEY HCDGGYERQG
TSSRVCQSSR QWSGSPPVCV PMKINVNVNS AAGLLDQFYE KRRLLIISAP DPSNRYYKMQ
ISMLQQSTCG LDLRHVTIIE LVGQPPQEVG RIREHQLSAN IIEELRQFQH LTRSYFNMVL
IDKQGIDRER YMEPVTPEEI FTFIDDYLLS NEELIQRREQ RDICD
