ID   CD99_HUMAN              Reviewed;         185 AA.
AC   P14209; A6NIW1; O00518; Q6ICV7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=CD99 antigen;
DE   AltName: Full=12E7;
DE   AltName: Full=E2 antigen;
DE   AltName: Full=Protein MIC2;
DE   AltName: Full=T-cell surface glycoprotein E2;
DE   AltName: CD_antigen=CD99;
DE   Flags: Precursor;
GN   Name=CD99; Synonyms=MIC2, MIC2X, MIC2Y;
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 [MRNA] (ISOFORM I), AND PROTEIN SEQUENCE OF 23-39.
RC   TISSUE=T-cell;
RX   PubMed=2479542; DOI=10.1002/j.1460-2075.1989.tb08485.x;
RA   Gelin C., Aubrit F., Phalipon A., Raynal B., Cole S., Kaczorek M.,
RA   Bernard A.;
RT   "The E2 antigen, a 32 kd glycoprotein involved in T-cell adhesion
RT   processes, is the MIC2 gene product.";
RL   EMBO J. 8:3253-3259(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
RA   Park S.H., Hahn J.H., Kim M.K., Sohn H.W., Choi E.Y., Kim S.H.;
RT   "An alternative splicing form of CD99 (MIC2).";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS I AND 3).
RC   TISSUE=Brain, Kidney, Lung carcinoma, Skin, and Uterus;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-105.
RX   PubMed=3472717; DOI=10.1101/sqb.1986.051.01.025;
RA   Darling S.M., Goodfellow P.J., Pym B., Banting G.S., Pritchard C.,
RA   Goodfellow P.N.;
RT   "Molecular genetics of MIC2: a gene shared by the human X and Y
RT   chromosomes.";
RL   Cold Spring Harb. Symp. Quant. Biol. 51:205-212(1986).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=2456574; DOI=10.1073/pnas.85.15.5605;
RA   Goodfellow P.J., Mondello C., Darling S.M., Pym B., Little P.,
RA   Goodfellow P.N.;
RT   "Absence of methylation of a CpG-rich region at the 5' end of the MIC2 gene
RT   on the active X, the inactive X, and the Y chromosome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5605-5609(1988).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND THR-181, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Involved in T-cell adhesion processes and in spontaneous
CC       rosette formation with erythrocytes. Plays a role in a late step of
CC       leukocyte extravasation helping leukocytes to overcome the endothelial
CC       basement membrane. Acts at the same site as, but independently of,
CC       PECAM1. Involved in T-cell adhesion processes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=I;
CC         IsoId=P14209-1; Sequence=Displayed;
CC       Name=II;
CC         IsoId=P14209-2; Sequence=VSP_004324;
CC       Name=3;
CC         IsoId=P14209-3; Sequence=VSP_046315;
CC   -!- PTM: Extensively O-glycosylated.
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}.
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DR   EMBL; X16996; CAA34863.1; -; mRNA.
DR   EMBL; U82164; AAB58501.1; -; mRNA.
DR   EMBL; CR450286; CAG29282.1; -; mRNA.
DR   EMBL; AC006209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471074; EAW98697.1; -; Genomic_DNA.
DR   EMBL; CH471074; EAW98698.1; -; Genomic_DNA.
DR   EMBL; BC002584; AAH02584.1; -; mRNA.
DR   EMBL; BC003147; AAH03147.1; -; mRNA.
DR   EMBL; BC010109; AAH10109.1; -; mRNA.
DR   EMBL; BC021620; AAH21620.1; -; mRNA.
DR   EMBL; BC024310; AAH24310.1; -; mRNA.
DR   EMBL; BQ948496; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M16279; AAA02999.1; -; mRNA.
DR   EMBL; J03841; AAA59848.1; -; Genomic_DNA.
DR   CCDS; CCDS14119.1; -. [P14209-1]
DR   CCDS; CCDS48071.1; -. [P14209-3]
DR   CCDS; CCDS75947.1; -. [P14209-2]
DR   PIR; S06786; A60592.
DR   RefSeq; NP_001116370.1; NM_001122898.2. [P14209-3]
DR   RefSeq; NP_001308296.1; NM_001321367.1. [P14209-2]
DR   RefSeq; NP_001308297.1; NM_001321368.1.
DR   RefSeq; NP_001308298.1; NM_001321369.1.
DR   RefSeq; NP_002405.1; NM_002414.4. [P14209-1]
DR   PDB; 7SFX; X-ray; 3.10 A; E/F=63-76.
DR   PDBsum; 7SFX; -.
DR   AlphaFoldDB; P14209; -.
DR   SMR; P14209; -.
DR   BioGRID; 110420; 77.
DR   IntAct; P14209; 16.
DR   MINT; P14209; -.
DR   STRING; 9606.ENSP00000370588; -.
DR   GlyConnect; 2923; 1 O-Linked glycan (1 site).
DR   GlyCosmos; P14209; 4 sites, 1 glycan.
DR   GlyGen; P14209; 8 sites, 3 O-linked glycans (8 sites).
DR   iPTMnet; P14209; -.
DR   PhosphoSitePlus; P14209; -.
DR   SwissPalm; P14209; -.
DR   BioMuta; CD99; -.
DR   DMDM; 119049; -.
DR   EPD; P14209; -.
DR   jPOST; P14209; -.
DR   MassIVE; P14209; -.
DR   MaxQB; P14209; -.
DR   PaxDb; 9606-ENSP00000370588; -.
DR   PeptideAtlas; P14209; -.
DR   ProteomicsDB; 1291; -.
DR   ProteomicsDB; 53032; -. [P14209-1]
DR   ProteomicsDB; 53033; -. [P14209-2]
DR   Pumba; P14209; -.
DR   ABCD; P14209; 1 sequenced antibody.
DR   Antibodypedia; 3499; 2007 antibodies from 49 providers.
DR   DNASU; 4267; -.
DR   Ensembl; ENST00000381187.8; ENSP00000370582.3; ENSG00000002586.20. [P14209-3]
DR   Ensembl; ENST00000381192.10; ENSP00000370588.3; ENSG00000002586.20. [P14209-1]
DR   Ensembl; ENST00000482405.7; ENSP00000494027.1; ENSG00000002586.20. [P14209-2]
DR   Ensembl; ENST00000611428.5; ENSP00000479999.1; ENSG00000002586.20. [P14209-2]
DR   Ensembl; ENST00000623253.4; ENSP00000485545.1; ENSG00000002586.20. [P14209-2]
DR   Ensembl; ENST00000711155.1; ENSP00000518644.1; ENSG00000292348.1. [P14209-2]
DR   Ensembl; ENST00000711159.1; ENSP00000518647.1; ENSG00000292348.1. [P14209-2]
DR   Ensembl; ENST00000711160.1; ENSP00000518648.1; ENSG00000292348.1. [P14209-1]
DR   Ensembl; ENST00000711164.1; ENSP00000518650.1; ENSG00000292348.1. [P14209-3]
DR   Ensembl; ENST00000711165.1; ENSP00000518651.1; ENSG00000292348.1. [P14209-2]
DR   GeneID; 4267; -.
DR   KEGG; hsa:4267; -.
DR   MANE-Select; ENST00000381192.10; ENSP00000370588.3; NM_002414.5; NP_002405.1.
DR   UCSC; uc004cqm.4; human. [P14209-1]
DR   AGR; HGNC:7082; -.
DR   CTD; 4267; -.
DR   DisGeNET; 4267; -.
DR   GeneCards; CD99; -.
DR   HGNC; HGNC:7082; CD99.
DR   HPA; ENSG00000002586; Low tissue specificity.
DR   MIM; 313470; gene.
DR   MIM; 450000; gene.
DR   neXtProt; NX_P14209; -.
DR   OpenTargets; ENSG00000002586; -.
DR   PharmGKB; PA30804; -.
DR   VEuPathDB; HostDB:ENSG00000002586; -.
DR   eggNOG; ENOG502S70S; Eukaryota.
DR   GeneTree; ENSGT00940000154344; -.
DR   HOGENOM; CLU_092825_1_1_1; -.
DR   InParanoid; P14209; -.
DR   OMA; HRNTNAE; -.
DR   OrthoDB; 4269940at2759; -.
DR   PhylomeDB; P14209; -.
DR   TreeFam; TF336273; -.
DR   PathwayCommons; P14209; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   SignaLink; P14209; -.
DR   BioGRID-ORCS; 4267; 6 hits in 622 CRISPR screens.
DR   ChiTaRS; CD99; human.
DR   GeneWiki; CD99; -.
DR   GenomeRNAi; 4267; -.
DR   Pharos; P14209; Tbio.
DR   PRO; PR:P14209; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Proteomes; UP000005640; Chromosome Y.
DR   RNAct; P14209; Protein.
DR   Bgee; ENSG00000002586; Expressed in type B pancreatic cell and 211 other cell types or tissues.
DR   ExpressionAtlas; P14209; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:SF15; CD99 ANTIGEN; 1.
DR   PANTHER; PTHR15076; CD99/MIC2 PROTEIN RELATED; 1.
DR   Pfam; PF12301; CD99L2; 1.
DR   Genevisible; P14209; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:2479542"
FT   CHAIN           23..185
FT                   /note="CD99 antigen"
FT                   /id="PRO_0000021726"
FT   TOPO_DOM        23..122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          27..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         34..49
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046315"
FT   VAR_SEQ         159..185
FT                   /note="AEQGEVDMESHRNANAEPAVQRTLLEK -> DG (in isoform II)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_004324"
FT   VARIANT         166
FT                   /note="M -> V (in dbSNP:rs4793)"
FT                   /id="VAR_014733"
FT   VARIANT         173
FT                   /note="N -> I (in dbSNP:rs4717)"
FT                   /id="VAR_014734"
SQ   SEQUENCE   185 AA;  18848 MW;  C302E09E6B022EAB CRC64;
     MARGAALALL LFGLLGVLVA APDGGFDLSD ALPDNENKKP TAIPKKPSAG DDFDLGDAVV
     DGENDDPRPP NPPKPMPNPN PNHPSSSGSF SDADLADGVS GGEGKGGSDG GGSHRKEGEE
     ADAPGVIPGI VGAVVVAVAG AISSFIAYQK KKLCFKENAE QGEVDMESHR NANAEPAVQR
     TLLEK
//