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CD99_MOUSE
ID   CD99_MOUSE              Reviewed;         175 AA.
AC   Q8VCN6; Q4L299; Q4L2A4; Q8BLN1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=CD99 antigen;
DE   AltName: Full=Paired immunoglobin-like type 2 receptor-ligand;
DE            Short=PILR-L;
DE   AltName: CD_antigen=CD99;
DE   Flags: Precursor;
GN   Name=Cd99; Synonyms=Pilrl;
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], TISSUE SPECIFICITY, AND INTERACTION WITH PILRB.
RX   PubMed=14970179; DOI=10.1084/jem.20031885;
RA   Shiratori I., Ogasawara K., Saito T., Lanier L.L., Arase H.;
RT   "Activation of natural killer cells and dendritic cells upon recognition of
RT   a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor.";
RL   J. Exp. Med. 199:525-533(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBUNIT.
RC   TISSUE=Testis;
RX   PubMed=15978751; DOI=10.1016/j.gene.2005.04.023;
RA   Park S.H., Shin Y.K., Suh Y.H., Park W.S., Ban Y.L., Choi H.S., Park H.J.,
RA   Jung K.C.;
RT   "Rapid divergency of rodent CD99 orthologs: implications for the evolution
RT   of the pseudoautosomal region.";
RL   Gene 353:177-188(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15280198; DOI=10.1182/blood-2004-03-1184;
RA   Bixel G., Kloep S., Butz S., Petri B., Engelhardt B., Vestweber D.;
RT   "Mouse CD99 participates in T-cell recruitment into inflamed skin.";
RL   Blood 104:3205-3213(2004).
RN   [6]
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).
CC   -!- FUNCTION: Involved in T-cell adhesion processes. Plays a role in a late
CC       step of leukocyte extravasation helping leukocytes to overcome the
CC       endothelial basement membrane. Acts at the same site as, but
CC       independently of, PECAM1. {ECO:0000269|PubMed:15280198,
CC       ECO:0000269|PubMed:20479283}.
CC   -!- SUBUNIT: Homodimer. Interacts with PILRB. {ECO:0000269|PubMed:14970179,
CC       ECO:0000269|PubMed:15978751}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with high levels in lung, spleen,
CC       thymus, liver and spinal chord. Expressed on leukocytes and endothelial
CC       cell contacts. Detected in a wide range of T-cells, including
CC       CD4-/CD8- and CD4+/CD8+ thymocytes. Expression is much lower in
CC       peripheral T-cells than in thymocytes. {ECO:0000269|PubMed:14970179,
CC       ECO:0000269|PubMed:15280198}.
CC   -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
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DR   EMBL; AY262359; AAP91691.1; -; Genomic_DNA.
DR   EMBL; AY262355; AAP91687.1; -; mRNA.
DR   EMBL; AK044051; BAC31754.1; -; mRNA.
DR   EMBL; BC019482; AAH19482.1; -; mRNA.
DR   RefSeq; NP_079860.2; NM_025584.2.
DR   AlphaFoldDB; Q8VCN6; -.
DR   IntAct; Q8VCN6; 3.
DR   PhosphoSitePlus; Q8VCN6; -.
DR   jPOST; Q8VCN6; -.
DR   MaxQB; Q8VCN6; -.
DR   PRIDE; Q8VCN6; -.
DR   ProteomicsDB; 283754; -.
DR   DNASU; 673094; -.
DR   GeneID; 673094; -.
DR   KEGG; mmu:673094; -.
DR   CTD; 4267; -.
DR   MGI; MGI:1913728; Cd99.
DR   InParanoid; Q8VCN6; -.
DR   PRO; PR:Q8VCN6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8VCN6; protein.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:MGI.
DR   GO; GO:0001773; P:myeloid dendritic cell activation; IDA:MGI.
DR   GO; GO:2000391; P:positive regulation of neutrophil extravasation; IMP:MGI.
DR   GO; GO:0072683; P: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   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..175
FT                   /note="CD99 antigen"
FT                   /id="PRO_0000226820"
FT   TOPO_DOM        29..137
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          30..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        100
FT                   /note="D -> G (in Ref. 3; BAC31754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="Missing (in Ref. 2; AAP91687/AAP91691 and 3;
FT                   BAC31754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="R -> P (in Ref. 2; AAP91687/AAP91691)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="G -> R (in Ref. 2; AAP91687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..149
FT                   /note="AA -> PP (in Ref. 3; BAC31754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   175 AA;  16783 MW;  A309E6E2494FBFE1 CRC64;
     MARAAMEAAA TVVLALALLG AAARGAASDD FNLGDALEDP NMKPTPKAPT PKKPSGGFDL
     EDALPGGGGG GAGEKPGNRP QPDPKPPRPH GDSGGISDSD LADAAGQGGG GAGRRGSGDE
     GGHGGAGGAE PEGTPQGLVP GVVAAVVAAV AGAVSSFVAY QRRRLCFREG GSAPV
 
 
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