PSG22_MOUSE
ID PSG22_MOUSE Reviewed; 475 AA.
AC Q810J1; Q66JZ0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pregnancy-specific glycoprotein 22 {ECO:0000312|MGI:MGI:1891354};
DE Flags: Precursor;
GN Name=Psg22 {ECO:0000312|MGI:MGI:1891354};
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 {ECO:0000312|EMBL:AAH50099.2};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [2] {ECO:0000312|EMBL:AAH50099.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH50099.2};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH50099.2, ECO:0000312|EMBL:AAH80694.1};
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, AND DEVELOPMENTAL STAGE.
RX PubMed=22423048; DOI=10.1095/biolreprod.111.098251;
RA Blois S.M., Tirado-Gonzalez I., Wu J., Barrientos G., Johnson B.,
RA Warren J., Freitag N., Klapp B.F., Irmak S., Ergun S., Dveskler G.S.;
RT "Early expression of pregnancy-specific glycoprotein 22 (PSG22) by
RT trophoblast cells modulates angiogenesis in mice.";
RL Biol. Reprod. 86:191-191(2012).
CC -!- FUNCTION: May have an angiogenic function during early placental
CC development. Binds to cell-surface heparan sulfate proteoglycans
CC (HSPGs), and stimulates secretion of the proangiogenic factors VEGFA
CC and TGFB from uterine dendritic cells and natural killer cells. Also
CC induces endothelial tube formation in vitro.
CC {ECO:0000269|PubMed:22423048}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in placental trophoblast giant cells
CC from 5.5 dpc onwards, with increased expression by 10.5 dpc (at protein
CC level). Also detected on the decidua basalis at 10.5 dpc (at protein
CC level). {ECO:0000269|PubMed:22423048}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CEA family.
CC {ECO:0000305}.
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DR EMBL; AC149065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050099; AAH50099.2; -; mRNA.
DR EMBL; BC080694; AAH80694.1; -; mRNA.
DR CCDS; CCDS20876.1; -.
DR RefSeq; NP_001004152.1; NM_001004152.2.
DR AlphaFoldDB; Q810J1; -.
DR STRING; 10090.ENSMUSP00000104121; -.
DR GlyGen; Q810J1; 3 sites.
DR PRIDE; Q810J1; -.
DR DNASU; 243862; -.
DR Ensembl; ENSMUST00000051973; ENSMUSP00000050633; ENSMUSG00000044903.
DR Ensembl; ENSMUST00000208221; ENSMUSP00000146795; ENSMUSG00000044903.
DR GeneID; 243862; -.
DR KEGG; mmu:243862; -.
DR UCSC; uc009fjq.1; mouse.
DR CTD; 243862; -.
DR MGI; MGI:1891354; Psg22.
DR VEuPathDB; HostDB:ENSMUSG00000044903; -.
DR eggNOG; ENOG502S42Z; Eukaryota.
DR GeneTree; ENSGT00960000186634; -.
DR OrthoDB; 998214at2759; -.
DR PhylomeDB; Q810J1; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 243862; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Psg22; mouse.
DR PRO; PR:Q810J1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q810J1; protein.
DR Bgee; ENSMUSG00000044903; Expressed in ectoplacental cone and 3 other tissues.
DR ExpressionAtlas; Q810J1; baseline and differential.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0045545; F:syndecan binding; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:MGI.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0071604; P:transforming growth factor beta production; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Pregnancy; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..475
FT /note="Pregnancy-specific glycoprotein 22"
FT /id="PRO_0000440673"
FT DOMAIN 44..140
FT /note="Ig-like V-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 162..260
FT /note="Ig-like V-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 280..380
FT /note="Ig-like V-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 387..471
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 406..454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 475 AA; 53225 MW; DBD0AF7EF014CC6A CRC64;
MEVSSELLSN GWTSWQRVLL TASLLTCWLL PITAGVTIES VPPKLVEGEN VLLRVDNLPE
NLRVFVWYRG VTDMSLGIAL YSLDYSTSVT GPKHSGRETL YRNGSLWIQN VTREDTGYYT
LQTISKNGKV VSNTSIFLQV NSSLFICGRP SPPALLTIES VPASVAEGGS VLLLVHSLPD
NLQSLLWYKG LTVFNKVEIA RHRTVKNSSE MGPAYSGREI VYSNGSLLLQ NVTWEDTGFY
TLQIVNRYWK MELAHIYLQV DTSLSSCCDD FNSVQLRINP VPPHAAEGER VLLQVHNLPE
DVQTFLWYKG VYSTQSFKIT EYSIVTESLI NGYAHSGREI LFINGSLLLQ DVTEKDSGFY
TLVTIDSNVK VETAHVQVNV NKLVTQPVMR VTDSTVRIQG SVVFTCFSDN TGVSIRWLFN
NQNLQLTERM TLSPSKCQLR IHTVRKEDAG EYQCEAFNPV SSKTSLPVRL TVMNE
