ID AX2R_HUMAN Reviewed; 193 AA. AC Q3ZCQ2; Q8NHX5; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 106. DE RecName: Full=Annexin-2 receptor; DE AltName: Full=Annexin II receptor; DE Short=AXIIR; GN Name=ANXA2R; Synonyms=AX2R, C5orf39; 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], POSSIBLE FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=16895901; DOI=10.1074/jbc.m607072200; RA Lu G., Maeda H., Reddy S.V., Kurihara N., Leach R., Anderson J.L., RA Roodman G.D.; RT "Cloning and characterization of the annexin II receptor on human marrow RT stromal cells."; RL J. Biol. Chem. 281:30542-30550(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-119. RC TISSUE=Placenta; 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 [4] RP IDENTIFICATION. RX PubMed=10359570; DOI=10.1172/jci6374; RA Menaa C., Devlin R.D., Reddy S.V., Gazitt Y., Choi S.J., Roodman G.D.; RT "Annexin II increases osteoclast formation by stimulating the proliferation RT of osteoclast precursors in human marrow cultures."; RL J. Clin. Invest. 103:1605-1613(1999). RN [5] 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: May act as a receptor for annexin II on marrow stromal cells CC to induce osteoclast formation. CC -!- INTERACTION: CC Q3ZCQ2; A5YKK6: CNOT1; NbExp=3; IntAct=EBI-21258284, EBI-1222758; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lymphocytes. CC Expressed in both resting CD4(+) and CD8(+) T-cells. CC {ECO:0000269|PubMed:16895901}. CC -!- CAUTION: PubMed:16895901 reports that it is a type I membrane protein. CC However, no clear transmembrane region is detected by prediction CC methods, suggesting that its localization at the plasma membrane is CC unsure. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY032883; AAK52335.1; -; mRNA. DR EMBL; AC025171; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC067873; AAH67873.1; -; mRNA. DR CCDS; CCDS34153.1; -. DR RefSeq; NP_001014301.1; NM_001014279.2. DR AlphaFoldDB; Q3ZCQ2; -. DR BioGRID; 133074; 8. DR IntAct; Q3ZCQ2; 6. DR STRING; 9606.ENSP00000315915; -. DR GlyGen; Q3ZCQ2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3ZCQ2; -. DR PhosphoSitePlus; Q3ZCQ2; -. DR BioMuta; ANXA2R; -. DR MassIVE; Q3ZCQ2; -. DR PaxDb; 9606-ENSP00000315915; -. DR PeptideAtlas; Q3ZCQ2; -. DR ProteomicsDB; 61907; -. DR Antibodypedia; 23232; 121 antibodies from 22 providers. DR DNASU; 389289; -. DR Ensembl; ENST00000314890.3; ENSP00000315915.3; ENSG00000177721.5. DR Ensembl; ENST00000616064.2; ENSP00000479862.1; ENSG00000177721.5. DR GeneID; 389289; -. DR KEGG; hsa:389289; -. DR MANE-Select; ENST00000616064.2; ENSP00000479862.1; NM_001014279.3; NP_001014301.1. DR UCSC; uc003jnf.4; human. DR AGR; HGNC:33463; -. DR CTD; 389289; -. DR DisGeNET; 389289; -. DR GeneCards; ANXA2R; -. DR HGNC; HGNC:33463; ANXA2R. DR HPA; ENSG00000177721; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 611296; gene. DR neXtProt; NX_Q3ZCQ2; -. DR OpenTargets; ENSG00000177721; -. DR PharmGKB; PA162380171; -. DR VEuPathDB; HostDB:ENSG00000177721; -. DR eggNOG; ENOG502TEGY; Eukaryota. DR GeneTree; ENSGT00390000009290; -. DR HOGENOM; CLU_1408354_0_0_1; -. DR InParanoid; Q3ZCQ2; -. DR OMA; FEWIGRT; -. DR OrthoDB; 5020485at2759; -. DR PhylomeDB; Q3ZCQ2; -. DR TreeFam; TF342039; -. DR PathwayCommons; Q3ZCQ2; -. DR SignaLink; Q3ZCQ2; -. DR BioGRID-ORCS; 389289; 17 hits in 1164 CRISPR screens. DR GenomeRNAi; 389289; -. DR Pharos; Q3ZCQ2; Tbio. DR PRO; PR:Q3ZCQ2; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q3ZCQ2; Protein. DR Bgee; ENSG00000177721; Expressed in granulocyte and 106 other cell types or tissues. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR InterPro; IPR031449; ANXA2R. DR PANTHER; PTHR38820; ANNEXIN-2 RECEPTOR; 1. DR PANTHER; PTHR38820:SF1; ANNEXIN-2 RECEPTOR; 1. DR Pfam; PF15721; ANXA2R; 1. DR Genevisible; Q3ZCQ2; HS. PE 1: Evidence at protein level; KW Receptor; Reference proteome. FT CHAIN 1..193 FT /note="Annexin-2 receptor" FT /id="PRO_0000295727" FT REGION 78..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..103 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 119 FT /note="Q -> R (in dbSNP:rs1054428)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_033348" FT VARIANT 186 FT /note="R -> W (in dbSNP:rs10971)" FT /id="VAR_033349" SQ SEQUENCE 193 AA; 21682 MW; 6BBC734AB14CE32F CRC64; MEQHFLGCVK RAWDSAEVAP EPQPPPIVSS EDRGPWPLPL YPVLGEYSLD SCDLGLLSSP CWRLPGVYWQ NGLSPGVQST LEPSTAKPTE FSWPGTQKQQ EAPVEEVGQA EEPDRLRLQQ LPWSSPLHPW DRQQDTEVCD SGCLLERRHP PALQPWRHLP GFSDCLEWIL RVGFAAFSVL WACCSRICGA KQP //