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   27-MAR-2024, entry version 160.
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   STRING; 9606.ENSP00000494087; -.
DR   iPTMnet; P55808; -.
DR   PhosphoSitePlus; P55808; -.
DR   BioMuta; XG; -.
DR   DMDM; 2499136; -.
DR   MassIVE; P55808; -.
DR   PeptideAtlas; P55808; -.
DR   ProteomicsDB; 56868; -. [P55808-1]
DR   ProteomicsDB; 56870; -. [P55808-3]
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   AGR; HGNC:12806; -.
DR   CTD; 7499; -.
DR   DisGeNET; 7499; -.
DR   GeneCards; XG; -.
DR   HGNC; HGNC:12806; XG.
DR   HPA; ENSG00000124343; Tissue enhanced (adipose tissue, 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; NKKLCFK; -.
DR   OrthoDB; 4339358at2759; -.
DR   PhylomeDB; P55808; -.
DR   TreeFam; TF336273; -.
DR   PathwayCommons; P55808; -.
DR   BioGRID-ORCS; 7499; 11 hits in 764 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 cell types or tissues.
DR   ExpressionAtlas; P55808; baseline and differential.
DR   GO; GO:0005886; C: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; CD99/MIC2 PROTEIN RELATED; 1.
DR   PANTHER; PTHR15076:SF4; GLYCOPROTEIN XG; 1.
DR   Pfam; PF12301; CD99L2; 1.
DR   Genevisible; P55808; HS.
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
//