C99L2_HUMAN
ID C99L2_HUMAN Reviewed; 262 AA.
AC Q8TCZ2; A8K2D5; A8K5R0; B3KWG2; B4DDL7; E7EMK5; E9PD27; Q8TAW2; Q8TCZ0;
AC Q8TCZ1; Q9BQG9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=CD99 antigen-like protein 2;
DE AltName: Full=MIC2-like protein 1;
DE AltName: CD_antigen=CD99;
DE Flags: Precursor;
GN Name=CD99L2; Synonyms=MIC2L1; ORFNames=UNQ1964/PRO4486;
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] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle, and Thymocyte;
RX PubMed=12706889; DOI=10.1016/s0378-1119(03)00401-3;
RA Suh Y.H., Shin Y.K., Kook M.-C., Oh K.I., Park W.S., Kim S.H., Lee I.-S.,
RA Park H.J., Huh T.-L., Park S.H.;
RT "Cloning, genomic organization, alternative transcripts and expression
RT analysis of CD99L2, a novel paralog of human CD99, and identification of
RT evolutionary conserved motifs.";
RL Gene 307:63-76(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 5 AND 6).
RC TISSUE=Brain, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Lung;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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: Plays a role in a late step of leukocyte extravasation
CC helping cells to overcome the endothelial basement membrane. Acts at
CC the same site as, but independently of, PECAM1 (By similarity).
CC Homophilic adhesion molecule, but these interactions may not be
CC required for cell aggregation (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8TCZ2; O43765: SGTA; NbExp=8; IntAct=EBI-2824782, EBI-347996;
CC Q8TCZ2; Q96EQ0: SGTB; NbExp=6; IntAct=EBI-2824782, EBI-744081;
CC Q8TCZ2; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-2824782, EBI-10262251;
CC Q8TCZ2; P55061: TMBIM6; NbExp=3; IntAct=EBI-2824782, EBI-1045825;
CC Q8TCZ2; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-2824782, EBI-11996766;
CC Q8TCZ2; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-2824782, EBI-741480;
CC Q8TCZ2; Q9UMX0-2: UBQLN1; NbExp=6; IntAct=EBI-2824782, EBI-10173939;
CC Q8TCZ2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2824782, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell
CC junction {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8TCZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCZ2-2; Sequence=VSP_034184;
CC Name=3;
CC IsoId=Q8TCZ2-3; Sequence=VSP_034182, VSP_034183;
CC Name=4;
CC IsoId=Q8TCZ2-4; Sequence=VSP_034181, VSP_034185;
CC Name=5;
CC IsoId=Q8TCZ2-5; Sequence=VSP_041815, VSP_041816;
CC Name=6;
CC IsoId=Q8TCZ2-6; Sequence=VSP_044663;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, with low expression in
CC thymus. {ECO:0000269|PubMed:12706889}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66515.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY078165; AAL86617.1; -; mRNA.
DR EMBL; AY078166; AAL86618.1; -; mRNA.
DR EMBL; AY078167; AAL86619.1; -; mRNA.
DR EMBL; AL136580; CAB66515.1; ALT_FRAME; mRNA.
DR EMBL; AY358837; AAQ89196.1; -; mRNA.
DR EMBL; AK290200; BAF82889.1; -; mRNA.
DR EMBL; AK291375; BAF84064.1; -; mRNA.
DR EMBL; AK293244; BAG56778.1; -; mRNA.
DR EMBL; AK125020; BAG54124.1; -; mRNA.
DR EMBL; AF002223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF274573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471169; EAW99391.1; -; Genomic_DNA.
DR EMBL; CH471169; EAW99392.1; -; Genomic_DNA.
DR EMBL; CH471169; EAW99393.1; -; Genomic_DNA.
DR EMBL; CH471169; EAW99395.1; -; Genomic_DNA.
DR EMBL; BC025729; AAH25729.1; -; mRNA.
DR EMBL; BC030536; AAH30536.1; -; mRNA.
DR CCDS; CCDS14697.1; -. [Q8TCZ2-3]
DR CCDS; CCDS14698.1; -. [Q8TCZ2-2]
DR CCDS; CCDS35427.1; -. [Q8TCZ2-1]
DR CCDS; CCDS55527.1; -. [Q8TCZ2-6]
DR CCDS; CCDS76044.1; -. [Q8TCZ2-5]
DR RefSeq; NP_001171737.1; NM_001184808.1. [Q8TCZ2-6]
DR RefSeq; NP_001229543.1; NM_001242614.1. [Q8TCZ2-5]
DR RefSeq; NP_113650.2; NM_031462.3. [Q8TCZ2-1]
DR RefSeq; NP_604394.1; NM_134445.3. [Q8TCZ2-3]
DR RefSeq; NP_604395.1; NM_134446.3. [Q8TCZ2-2]
DR RefSeq; XP_011529504.1; XM_011531202.2. [Q8TCZ2-4]
DR AlphaFoldDB; Q8TCZ2; -.
DR BioGRID; 123726; 38.
DR IntAct; Q8TCZ2; 26.
DR STRING; 9606.ENSP00000480322; -.
DR GlyGen; Q8TCZ2; 3 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; Q8TCZ2; -.
DR PhosphoSitePlus; Q8TCZ2; -.
DR SwissPalm; Q8TCZ2; -.
DR BioMuta; CD99L2; -.
DR DMDM; 74730601; -.
DR EPD; Q8TCZ2; -.
DR jPOST; Q8TCZ2; -.
DR MassIVE; Q8TCZ2; -.
DR MaxQB; Q8TCZ2; -.
DR PaxDb; Q8TCZ2; -.
DR PeptideAtlas; Q8TCZ2; -.
DR PRIDE; Q8TCZ2; -.
DR ProteomicsDB; 19570; -.
DR ProteomicsDB; 74199; -. [Q8TCZ2-1]
DR ProteomicsDB; 74200; -. [Q8TCZ2-2]
DR ProteomicsDB; 74201; -. [Q8TCZ2-3]
DR ProteomicsDB; 74203; -. [Q8TCZ2-5]
DR TopDownProteomics; Q8TCZ2-1; -. [Q8TCZ2-1]
DR Antibodypedia; 50585; 180 antibodies from 22 providers.
DR DNASU; 83692; -.
DR Ensembl; ENST00000346693.8; ENSP00000489222.1; ENSG00000102181.21. [Q8TCZ2-4]
DR Ensembl; ENST00000355149.8; ENSP00000347275.3; ENSG00000102181.21. [Q8TCZ2-3]
DR Ensembl; ENST00000370377.8; ENSP00000359403.3; ENSG00000102181.21. [Q8TCZ2-1]
DR Ensembl; ENST00000437787.6; ENSP00000394858.2; ENSG00000102181.21. [Q8TCZ2-6]
DR Ensembl; ENST00000466436.5; ENSP00000417697.1; ENSG00000102181.21. [Q8TCZ2-2]
DR Ensembl; ENST00000613030.4; ENSP00000480322.1; ENSG00000102181.21. [Q8TCZ2-5]
DR GeneID; 83692; -.
DR KEGG; hsa:83692; -.
DR MANE-Select; ENST00000370377.8; ENSP00000359403.3; NM_031462.4; NP_113650.2.
DR UCSC; uc004fek.4; human. [Q8TCZ2-1]
DR CTD; 83692; -.
DR DisGeNET; 83692; -.
DR GeneCards; CD99L2; -.
DR HGNC; HGNC:18237; CD99L2.
DR HPA; ENSG00000102181; Tissue enhanced (skeletal).
DR MIM; 300846; gene.
DR neXtProt; NX_Q8TCZ2; -.
DR OpenTargets; ENSG00000102181; -.
DR PharmGKB; PA30805; -.
DR VEuPathDB; HostDB:ENSG00000102181; -.
DR eggNOG; ENOG502RZ6C; Eukaryota.
DR GeneTree; ENSGT00940000154344; -.
DR HOGENOM; CLU_092825_0_1_1; -.
DR InParanoid; Q8TCZ2; -.
DR OMA; EDIAWGG; -.
DR OrthoDB; 1559463at2759; -.
DR PhylomeDB; Q8TCZ2; -.
DR TreeFam; TF332323; -.
DR PathwayCommons; Q8TCZ2; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; Q8TCZ2; -.
DR BioGRID-ORCS; 83692; 4 hits in 698 CRISPR screens.
DR ChiTaRS; CD99L2; human.
DR GeneWiki; CD99L2; -.
DR GenomeRNAi; 83692; -.
DR Pharos; Q8TCZ2; Tbio.
DR PRO; PR:Q8TCZ2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8TCZ2; protein.
DR Bgee; ENSG00000102181; Expressed in prefrontal cortex and 172 other tissues.
DR ExpressionAtlas; Q8TCZ2; baseline and differential.
DR Genevisible; Q8TCZ2; HS.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl.
DR GO; GO:2000409; P:positive regulation of T cell extravasation; IEA:Ensembl.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 2.
DR Pfam; PF12301; CD99L2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..262
FT /note="CD99 antigen-like protein 2"
FT /id="PRO_0000340092"
FT TOPO_DOM 26..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 38..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 44..145
FT /note="QPWDHTTTTTTNRPGTTRAPAKPPGSGLDLADALDDQDDGRRKPGIGGRERW
FT NHVTTTTKRPVTTRAPANTLGNDFDLADALDDRNDRDDGRRKPIAGGGGF -> PALGM
FT YHKLDGLKQQNFILSLFWMLEVLYQGVGWATFSLKALGKNLSLTFPTSGGSRCSLVCGC
FT ITPISASVVTWCSPFCVSLLSLTKMLVSGFKAHLDNPG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034181"
FT VAR_SEQ 44
FT /note="Q -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12706889"
FT /id="VSP_034182"
FT VAR_SEQ 45..116
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12706889"
FT /id="VSP_034183"
FT VAR_SEQ 45..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12706889,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_034184"
FT VAR_SEQ 68
FT /note="G -> GPTEG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041815"
FT VAR_SEQ 93..165
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044663"
FT VAR_SEQ 146..262
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034185"
FT VAR_SEQ 218..219
FT /note="QQ -> QHAAAGQE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041816"
FT CONFLICT 109
FT /note="R -> I (in Ref. 4; BAF82889)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> Q (in Ref. 4; BAG54124)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Y -> H (in Ref. 4; BAF82889)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> R (in Ref. 4; BAF84064)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> G (in Ref. 4; BAG56778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 27986 MW; 3A254961DD32C191 CRC64;
MVAWRSAFLV CLAFSLATLV QRGSGDFDDF NLEDAVKETS SVKQPWDHTT TTTTNRPGTT
RAPAKPPGSG LDLADALDDQ DDGRRKPGIG GRERWNHVTT TTKRPVTTRA PANTLGNDFD
LADALDDRND RDDGRRKPIA GGGGFSDKDL EDIVGGGEYK PDKGKGDGRY GSNDDPGSGM
VAEPGTIAGV ASALAMALIG AVSSYISYQQ KKFCFSIQQG LNADYVKGEN LEAVVCEEPQ
VKYSTLHTQS AEPPPPPEPA RI
