XG_HUMAN
ID XG_HUMAN Reviewed; 180 AA.
AC P55808; E9PCH1; Q496N8; Q496N9; Q496P0; Q71BZ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glycoprotein Xg;
DE AltName: Full=Protein PBDX;
DE Flags: Precursor;
GN Name=XG; Synonyms=PBDX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Bone marrow;
RX PubMed=8054981; DOI=10.1038/ng0494-394;
RA Ellis N.A., Ye T.Z., Patton S., German J., Goodfellow P.N., Weller P.;
RT "Cloning of PBDX, an MIC2-related gene that spans the pseudoautosomal
RT boundary on chromosome Xp.";
RL Nat. Genet. 6:394-400(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Naoko S., Fujiki K., Kanai A., Tanaka Y., Iwata T.;
RT "Identification of PBDX gene highly expressed in human cornea.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Naoko S., Tanaka Y., Iwata T.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP ASN-60.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=7533029; DOI=10.1038/ng1194-285;
RA Ellis N.A., Tippett P., Petty A., Reid M., Weller P.A., Ye T.Z., German J.,
RA Goodfellow P.N., Thomas S., Banting G.;
RT "PBDX is the XG blood group gene.";
RL Nat. Genet. 8:285-290(1994).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10688843;
RA Fouchet C., Gane P., Huet M., Fellous M., Rouger P., Banting G.,
RA Cartron J.P., Lopez C.;
RT "A study of the coregulation and tissue specificity of XG and MIC2 gene
RT expression in eukaryotic cells.";
RL Blood 95:1819-1826(2000).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7533029};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:7533029}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P55808-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55808-2; Sequence=VSP_037319;
CC Name=3;
CC IsoId=P55808-3; Sequence=VSP_037320;
CC -!- TISSUE SPECIFICITY: Expressed in erythroid tissues, including thymus,
CC bone marrow and fetal liver, and in several nonerythroid tissues, such
CC as heart, placenta, skeletal muscle, thyroid and trachea, as well as in
CC skin fibroblasts. Expression is low or undetectable in other tissues.
CC {ECO:0000269|PubMed:10688843}.
CC -!- PTM: O-glycosylated. {ECO:0000305}.
CC -!- POLYMORPHISM: XG is responsible for the Xg blood group system.
CC {ECO:0000305|PubMed:10688843}.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=xg";
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DR EMBL; X96421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF380356; AAL04055.1; -; mRNA.
DR EMBL; AF534880; AAN03481.1; -; mRNA.
DR EMBL; AC006209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100765; AAI00766.1; -; mRNA.
DR EMBL; BC100766; AAI00767.1; -; mRNA.
DR EMBL; BC100767; AAI00768.1; -; mRNA.
DR CCDS; CCDS14120.1; -. [P55808-1]
DR CCDS; CCDS48073.1; -. [P55808-3]
DR PIR; S43791; S43791.
DR RefSeq; NP_001135391.1; NM_001141919.1. [P55808-3]
DR RefSeq; NP_001135392.1; NM_001141920.1. [P55808-2]
DR RefSeq; NP_780778.1; NM_175569.2. [P55808-1]
DR AlphaFoldDB; P55808; -.
DR iPTMnet; P55808; -.
DR PhosphoSitePlus; P55808; -.
DR BioMuta; XG; -.
DR DMDM; 2499136; -.
DR MassIVE; P55808; -.
DR PeptideAtlas; P55808; -.
DR PRIDE; P55808; -.
DR Antibodypedia; 7780; 52 antibodies from 15 providers.
DR DNASU; 7499; -.
DR Ensembl; ENST00000381174.10; ENSP00000370566.5; ENSG00000124343.14. [P55808-1]
DR Ensembl; ENST00000644266.2; ENSP00000494087.1; ENSG00000124343.14. [P55808-3]
DR GeneID; 7499; -.
DR KEGG; hsa:7499; -.
DR MANE-Select; ENST00000644266.2; ENSP00000494087.1; NM_001141919.2; NP_001135391.1. [P55808-3]
DR UCSC; uc004cqp.5; human. [P55808-1]
DR CTD; 7499; -.
DR DisGeNET; 7499; -.
DR GeneCards; XG; -.
DR HGNC; HGNC:12806; XG.
DR HPA; ENSG00000124343; Tissue enhanced (skin).
DR MIM; 300879; gene.
DR MIM; 314700; phenotype.
DR neXtProt; NX_P55808; -.
DR OpenTargets; ENSG00000124343; -.
DR PharmGKB; PA37405; -.
DR VEuPathDB; HostDB:ENSG00000124343; -.
DR eggNOG; ENOG502TEY7; Eukaryota.
DR GeneTree; ENSGT00510000049811; -.
DR HOGENOM; CLU_1582194_0_0_1; -.
DR InParanoid; P55808; -.
DR OMA; NHGGNTD; -.
DR OrthoDB; 1536754at2759; -.
DR PhylomeDB; P55808; -.
DR TreeFam; TF336273; -.
DR PathwayCommons; P55808; -.
DR BioGRID-ORCS; 7499; 10 hits in 691 CRISPR screens.
DR ChiTaRS; XG; human.
DR GenomeRNAi; 7499; -.
DR Pharos; P55808; Tdark.
DR PRO; PR:P55808; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P55808; protein.
DR Bgee; ENSG00000124343; Expressed in calcaneal tendon and 133 other tissues.
DR ExpressionAtlas; P55808; baseline and differential.
DR Genevisible; P55808; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IBA:GO_Central.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IBA:GO_Central.
DR GO; GO:0072683; P:T cell extravasation; IBA:GO_Central.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 1.
DR Pfam; PF12301; CD99L2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Blood group antigen; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..180
FT /note="Glycoprotein Xg"
FT /id="PRO_0000022693"
FT TOPO_DOM 22..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 85
FT /note="G -> GS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037319"
FT VAR_SEQ 125
FT /note="G -> GRGGYRLNSRYGNTYG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037320"
FT VARIANT 60
FT /note="D -> N (in dbSNP:rs5939319)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054063"
FT CONFLICT P55808-3:131
FT /note="L -> P (in Ref. 5; AAI00766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19723 MW; DADAA9E6859C4530 CRC64;
MESWWGLPCL AFLCFLMHAR GQRDFDLADA LDDPEPTKKP NSDIYPKPKP PYYPQPENPD
SGGNIYPRPK PRPQPQPGNS GNSGGYFNDV DRDDGRYPPR PRPRPPAGGG GGGYSSYGNS
DNTHGGDHHS TYGNPEGNMV AKIVSPIVSV VVVTLLGAAA SYFKLNNRRN CFRTHEPENV
