C99L2_MOUSE
ID C99L2_MOUSE Reviewed; 237 AA.
AC Q8BIF0; A2AP77; Q8R447;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
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 [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=18163232; DOI=10.1080/15419060701755966;
RA Schenkel A.R., Dufour E.M., Chew T.W., Sorg E., Muller W.A.;
RT "The murine CD99-related molecule CD99-like 2 (CD99L2) is an adhesion
RT molecule involved in the inflammatory response.";
RL Cell Commun. Adhes. 14:227-237(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=17344467; DOI=10.1182/blood-2006-08-043109;
RA Bixel M.G., Petri B., Khandoga A.G., Khandoga A., Wolburg-Buchholz K.,
RA Wolburg H., Marz S., Krombach F., Vestweber D.;
RT "A CD99-related antigen on endothelial cells mediates neutrophil but not
RT lymphocyte extravasation in vivo.";
RL Blood 109:5327-5336(2007).
RN [7]
RP FUNCTION.
RX PubMed=20479283; DOI=10.1182/blood-2009-12-256388;
RA Bixel M.G., Li H., Petri B., Khandoga A.G., Khandoga A., Zarbock A.,
RA Wolburg-Buchholz K., Wolburg H., Sorokin L., Zeuschner D., Maerz S.,
RA Butz S., Krombach F., Vestweber D.;
RT "CD99 and CD99L2 act at the same site as, but independently of, PECAM-1
RT during leukocyte diapedesis.";
RL Blood 116:1172-1184(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Homophilic adhesion
CC molecule, but these interactions may not be required for cell
CC aggregation. {ECO:0000269|PubMed:17344467, ECO:0000269|PubMed:18163232,
CC ECO:0000269|PubMed:20479283}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell
CC junction {ECO:0000269|PubMed:17344467}. Note=Concentrated at cell-cell
CC contacts in cultured endothelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long isoform;
CC IsoId=Q8BIF0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short isoform;
CC IsoId=Q8BIF0-2; Sequence=VSP_034186;
CC -!- TISSUE SPECIFICITY: Highly expressed in the nervous system, including
CC brain, dentate nucleus of hippocampus, granular and Purkinje cells of
CC cerebellum, brain stem nucleus and choroid plexus. Expressed in
CC peripheral blood T- and B-cells and neutrophils (at protein level).
CC Almost undetectable in bone marrow-derived neutrophils (at protein
CC level). Also expressed in thymocytes (at protein level) with higher
CC expression in cortical thymocytes than in medullary thymocytes.
CC Expressed at high levels in testis (mostly in germ cells and Sertoli
CC cells) and ovary (mostly in granulosa cells). Expressed in lung, heart,
CC kidney and liver (at protein level); however, expression in heart,
CC kidney and liver seems restricted to endothelial cells (at protein
CC level). Highly expressed in endothelial cells and to a lower level in
CC vascular smooth muscle cells (at protein level). Low expression in
CC spleen. {ECO:0000269|PubMed:12706889, ECO:0000269|PubMed:17344467,
CC ECO:0000269|PubMed:18163232}.
CC -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expressed in most tissues, especially
CC in the nervous system, including the cerebral cortex, cerebellum,
CC spinal cord and ganglion. There is no change in expression pattern from
CC 12.5 dpc to neonatal day 1. Highly expressed in the subventricular zone
CC and cortical plate of fetal brain and in the dorsal root ganglion of
CC the peripheral nervous system. Except in the nervous system, expression
CC in adult tissues is weaker than in fetal ones.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:17344467}.
CC -!- MISCELLANEOUS: [Isoform 2]: Seems to be the major transcript.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM25451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY078163; AAL86615.1; -; mRNA.
DR EMBL; EF516990; ABP73253.1; -; mRNA.
DR EMBL; AK080225; BAC37853.1; -; mRNA.
DR EMBL; AK166275; BAE38674.1; -; mRNA.
DR EMBL; AL833776; CAM25449.1; -; Genomic_DNA.
DR EMBL; AL772294; CAM25449.1; JOINED; Genomic_DNA.
DR EMBL; AL833776; CAM25450.1; -; Genomic_DNA.
DR EMBL; AL772294; CAM25450.1; JOINED; Genomic_DNA.
DR EMBL; AL833776; CAM25451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772294; CAM25451.1; JOINED; Genomic_DNA.
DR EMBL; BC031736; AAH31736.1; -; mRNA.
DR CCDS; CCDS30179.1; -. [Q8BIF0-2]
DR CCDS; CCDS57761.1; -. [Q8BIF0-1]
DR RefSeq; NP_001186278.1; NM_001199349.1. [Q8BIF0-1]
DR RefSeq; NP_612182.1; NM_138309.3. [Q8BIF0-2]
DR AlphaFoldDB; Q8BIF0; -.
DR BioGRID; 228600; 1.
DR iPTMnet; Q8BIF0; -.
DR PhosphoSitePlus; Q8BIF0; -.
DR SwissPalm; Q8BIF0; -.
DR MaxQB; Q8BIF0; -.
DR PaxDb; Q8BIF0; -.
DR PeptideAtlas; Q8BIF0; -.
DR PRIDE; Q8BIF0; -.
DR ProteomicsDB; 265269; -. [Q8BIF0-1]
DR ProteomicsDB; 265270; -. [Q8BIF0-2]
DR Antibodypedia; 50585; 180 antibodies from 22 providers.
DR DNASU; 171486; -.
DR Ensembl; ENSMUST00000037391; ENSMUSP00000042606; ENSMUSG00000035776. [Q8BIF0-1]
DR Ensembl; ENSMUST00000080035; ENSMUSP00000078944; ENSMUSG00000035776. [Q8BIF0-2]
DR GeneID; 171486; -.
DR KEGG; mmu:171486; -.
DR UCSC; uc009tjz.2; mouse. [Q8BIF0-2]
DR UCSC; uc009tka.2; mouse. [Q8BIF0-1]
DR CTD; 83692; -.
DR MGI; MGI:2177151; Cd99l2.
DR VEuPathDB; HostDB:ENSMUSG00000035776; -.
DR eggNOG; ENOG502RZ6C; Eukaryota.
DR GeneTree; ENSGT00940000154344; -.
DR InParanoid; Q8BIF0; -.
DR OMA; EDIAWGG; -.
DR OrthoDB; 1559463at2759; -.
DR PhylomeDB; Q8BIF0; -.
DR TreeFam; TF332323; -.
DR BioGRID-ORCS; 171486; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cd99l2; mouse.
DR PRO; PR:Q8BIF0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BIF0; protein.
DR Bgee; ENSMUSG00000035776; Expressed in rostral migratory stream and 267 other tissues.
DR ExpressionAtlas; Q8BIF0; baseline and differential.
DR Genevisible; Q8BIF0; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050904; P:diapedesis; IMP:MGI.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IMP:MGI.
DR GO; GO:2000409; P:positive regulation of T cell extravasation; IMP:MGI.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 1.
DR Pfam; PF12301; CD99L2; 1.
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..237
FT /note="CD99 antigen-like protein 2"
FT /id="PRO_0000340093"
FT TOPO_DOM 26..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 47..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 49..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12706889"
FT /id="VSP_034186"
SQ SEQUENCE 237 AA; 25463 MW; 6876EB515DFA426A CRC64;
MVARLTAFLV CLVFSLATLV QRGYGDTDGF NLEDALKETS SVKQRWDHFS TTTRRPVTTR
APANPAERWD HVATTTTRRP GTTRAPSNPM ELDGFDLEDA LDDRNDLDGP KKPSAGEAGG
WSDKDLEDIV EGGGYKPDKN KGGGGYGSND DPGSGISTET GTIAGVASAL AMALIGAVSS
YISYQQKKFC FSIQQGLNAD YVKGENLEAV VCEEPQVTYS KQETQSAEPP PPEPPRI
