SRPX2_MOUSE
ID SRPX2_MOUSE Reviewed; 468 AA.
AC Q8R054; B1AVI6; Q3UVU0; Q8K1F8; Q8K4W6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sushi repeat-containing protein SRPX2;
DE Flags: Precursor;
GN Name=Srpx2;
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 [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 59-468.
RC TISSUE=Kidney;
RA Huang C.-H., Chen H., Peng J., Chen Y.;
RT "Cloning and characterization of the sushi-repeat containing protein (SRP)
RT as a novel interaction partner of Rh type C glycoprotein (RhCG).";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [5]
RP FUNCTION, INTERACTION WITH PLAUR, AND TISSUE SPECIFICITY.
RX PubMed=19667118; DOI=10.1096/fj.09-135202;
RA Miljkovic-Licina M., Hammel P., Garrido-Urbani S., Bradfield P.F.,
RA Szepetowski P., Imhof B.A.;
RT "Sushi repeat protein X-linked 2, a novel mediator of angiogenesis.";
RL FASEB J. 23:4105-4116(2009).
RN [6]
RP FUNCTION.
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. Promotes synapse formation. Required for ultrasonic vocalizations.
CC {ECO:0000269|PubMed:19667118, 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell surface {ECO:0000250}. Synapse {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in angiogenic endothelial cells (at
CC protein level). {ECO:0000269|PubMed:19667118}.
CC -!- PTM: Contains chondroitin sulfate chains. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE23179.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF393640; AAM73691.1; -; mRNA.
DR EMBL; AF393647; AAM73690.1; -; Genomic_DNA.
DR EMBL; AF393641; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AF393642; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AF393643; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AF393644; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AF393645; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AF393646; AAM73690.1; JOINED; Genomic_DNA.
DR EMBL; AK136935; BAE23179.1; ALT_INIT; mRNA.
DR EMBL; AL691421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028307; AAH28307.1; ALT_INIT; mRNA.
DR CCDS; CCDS41119.2; -.
DR RefSeq; NP_001077364.2; NM_001083895.3.
DR RefSeq; NP_081114.2; NM_026838.4.
DR AlphaFoldDB; Q8R054; -.
DR SMR; Q8R054; -.
DR STRING; 10090.ENSMUSP00000108929; -.
DR iPTMnet; Q8R054; -.
DR PhosphoSitePlus; Q8R054; -.
DR MaxQB; Q8R054; -.
DR PaxDb; Q8R054; -.
DR PeptideAtlas; Q8R054; -.
DR PRIDE; Q8R054; -.
DR ProteomicsDB; 257364; -.
DR Antibodypedia; 28519; 174 antibodies from 31 providers.
DR Ensembl; ENSMUST00000033606; ENSMUSP00000033606; ENSMUSG00000031253.
DR Ensembl; ENSMUST00000113304; ENSMUSP00000108929; ENSMUSG00000031253.
DR GeneID; 68792; -.
DR KEGG; mmu:68792; -.
DR UCSC; uc009ufd.3; mouse.
DR CTD; 27286; -.
DR MGI; MGI:1916042; Srpx2.
DR VEuPathDB; HostDB:ENSMUSG00000031253; -.
DR eggNOG; ENOG502QREP; Eukaryota.
DR GeneTree; ENSGT00940000159149; -.
DR HOGENOM; CLU_047011_0_0_1; -.
DR InParanoid; Q8R054; -.
DR OMA; EQRDMCE; -.
DR OrthoDB; 544541at2759; -.
DR PhylomeDB; Q8R054; -.
DR TreeFam; TF336515; -.
DR BioGRID-ORCS; 68792; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Srpx2; mouse.
DR PRO; PR:Q8R054; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8R054; protein.
DR Bgee; ENSMUSG00000031253; Expressed in vault of skull and 127 other tissues.
DR Genevisible; Q8R054; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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; IPI: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; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0071625; P:vocalization behavior; IMP: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 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..468
FT /note="Sushi repeat-containing protein SRPX2"
FT /id="PRO_0000274526"
FT DOMAIN 72..122
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 123..181
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 180..264
FT /note="HYR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00113"
FT DOMAIN 265..324
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 74..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 94..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 125..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 152..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 267..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 295..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 59
FT /note="P -> H (in Ref. 1; AAM73691/AAM73690)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="G -> S (in Ref. 2; BAE23179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53140 MW; C48D645CC4B0DF3D CRC64;
MMTSPLTQRG ALSLLLLLMP AVTPTWYAGS GYSPDESYNE VYAEEVPAAR ARALDYRVPR
WCYTLNIQDG EATCYSPRGG NYHSSLGTRC ELSCDRGFRL IGRKSVQCLP SRRWSGTAYC
RQIRCHTLPF ITSGTYTCTN GMLLDSRCDY SCSSGYHLEG DRSRICMEDG RWSGGEPVCV
DIDPPKIRCP HSREKMAEPE KLTARVYWDP PLVKDSADGT ITRVTLRGPE PGSHFPEGEH
VIRYTAYDRA YNRASCKFIV KVQVRRCPIL KPPQHGYLTC SSAGDNYGAI CEYHCDGGYE
RQGTPSRVCQ SSRQWSGTPP VCTPMKINVN VNSAAGLLDQ FYEKQRLLIV SAPDPSNRYY
KMQISMLQQS TCGLDLRHVT IIELVGQPPQ EVGRIREQQL SAGIIEELRQ FQRLTRSYFN
MVLIDKQGID RERYMEPVTP EEIFTFIDDY LLSNEELARR VEQRDLCE
