{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P61073","secondaryAccessions":["B2R5N0","O60835","P30991","P56438","Q53S69","Q9BXA0","Q9UKN2"],"uniProtkbId":"CXCR4_HUMAN","entryAudit":{"firstPublicDate":"2004-04-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-04-26","entryVersion":212,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"C-X-C chemokine receptor type 4"},"shortNames":[{"value":"CXC-R4"},{"value":"CXCR-4"}]},"alternativeNames":[{"fullName":{"value":"FB22"}},{"fullName":{"value":"Fusin"}},{"fullName":{"value":"HM89"}},{"fullName":{"value":"LCR1"}},{"fullName":{"value":"Leukocyte-derived seven transmembrane domain receptor"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8276799"}],"value":"LESTR"}]},{"fullName":{"value":"Lipopolysaccharide-associated protein 3"},"shortNames":[{"value":"LAP-3"},{"value":"LPS-associated protein 3"}]},{"fullName":{"value":"NPYRL"}},{"fullName":{"value":"Stromal cell-derived factor 1 receptor"},"shortNames":[{"value":"SDF-1 receptor"}]}],"cdAntigenNames":[{"value":"CD184"}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9468539"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2561"}],"value":"CXCR4"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P70658"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10074102"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10452968"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10644702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10825158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11276205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16725153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17197449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18799424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20048153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20228059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20505072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24912431"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28978524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39093700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8752280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8752281"}],"value":"Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10074102, PubMed:10452968, PubMed:10644702, PubMed:10825158, PubMed:18799424, PubMed:20048153, PubMed:20505072, PubMed:24912431, PubMed:28978524, PubMed:8752280, PubMed:8752281). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:16725153, PubMed:17197449, PubMed:18799424, PubMed:39093700). CXCR4 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (PubMed:17197449, PubMed:39093700). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Also acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation (By similarity). Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells (By similarity). Involved in cerebellar development; in the CNS, could mediate hippocampal-neuron surviva (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10074122"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10756055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8849450"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8929542"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9427609"}],"value":"(Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:10074122, PubMed:10756055, PubMed:8849450, PubMed:8929542, PubMed:9427609)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10644702"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10825158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11276205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12034737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16725153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17077324"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18799424"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18834145"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19116316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20048153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20215400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20228059"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20505072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28978524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37209686"}],"value":"Monomer. Can form homodimers (PubMed:20929726). Interacts with CD164 (PubMed:17077324). Interacts (when phosphorylated) with ARRB1; the interaction is associated with internalization of the receptor and short-term desensitization to the ligand (PubMed:37209686). Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with ARR3; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates calcium mobilization (PubMed:20048153). Interacts with RNF113A; the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and subsequent degradation (PubMed:28978524). Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10074122"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10756055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11027346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25612609"}],"value":"(Microbial infection) Interacts with HIV-1 surface protein gp120 and Tat"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9427609"}],"value":"(Microbial infection) Interacts with HHV-8 protein ORF K4 (PubMed:25612609)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22496149"}],"value":"(Microbial infection) May interact with human cytomegalovirus/HHV-5 protein UL78"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19308288"}],"value":"(Microbial infection) Interacts with Staphylococcus aureus protein SSL10"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P25106","geneName":"ACKR3","intActId":"EBI-1965291"},"numberOfExperiments":18,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P51681","geneName":"CCR5","intActId":"EBI-489374"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"Q04900","geneName":"CD164","intActId":"EBI-2115896"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P04233","geneName":"CD74","intActId":"EBI-2622890"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P49682","geneName":"CXCR3","intActId":"EBI-12836456"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P32302","geneName":"CXCR5","intActId":"EBI-2835269"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"Q16643","geneName":"DBN1","intActId":"EBI-351394"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"Q96J02-2","geneName":"ITCH","intActId":"EBI-6672198"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"P35579","geneName":"MYH9","intActId":"EBI-350338"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"O60896","geneName":"RAMP3","intActId":"EBI-720447"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"O60603","geneName":"TLR2","intActId":"EBI-973722"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P61073","intActId":"EBI-489411"},"interactantTwo":{"uniProtKBAccession":"Q07266-1","geneName":"Dbn1","intActId":"EBI-8786792"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10452968"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14602072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20215400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21540189"}],"value":"In unstimulated cells, diffuse pattern on plasma membrane (PubMed:10452968, PubMed:14602072, PubMed:21540189). On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (PubMed:14602072). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (PubMed:20215400)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10452968"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14602072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21540189"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20929726"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20215400"}],"value":"Cell junction","id":"SL-0038"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21540189"}],"value":"Early endosome","id":"SL-0094"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21540189"}],"value":"Late endosome","id":"SL-0152"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21540189"}],"value":"Lysosome","id":"SL-0158"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P61073-1","P30991-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"CXCR4-LO"}],"isoformIds":["P61073-2","P30991-2"],"sequenceIds":["VSP_001890"],"isoformSequenceStatus":"Described"}],"note":{"texts":[{"value":"Additional isoforms seem to exist."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11276205"}],"value":"Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22496149"}],"value":"(Microbial infection) May be down-regulated by Human cytomegalovirus/HHV-5"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11027346"}],"value":"(Microbial infection) May be down-regulated by HIV-1 tat"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10074122"}],"value":"The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37209686"}],"value":"The P-X-P-P motif is phosphorylated in response to ligand binding, promoting. association with beta-arrestin ARRB1"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14602072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19116316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20048153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37209686"}],"value":"Phosphorylated on agonist stimulation (PubMed:20048153, PubMed:37209686). Phosphorylation of the P-X-P-P motif promotes association with beta-arrestin ARRB1, leading to receptor desensitization and negative regulation of G protein-coupled receptor signaling (PubMed:37209686). Phosphorylation at Ser-324 and Ser-325 leads to recruitment of ITCH, ubiquitination and protein degradation (PubMed:14602072, PubMed:19116316)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14602072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28978524"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34927784"}],"value":"Ubiquitinated after ligand binding, leading to its degradation (PubMed:28978524). Ubiquitinated by ITCH at the cell membrane on agonist stimulation (PubMed:14602072, PubMed:34927784). The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10089882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12034737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16725153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18834145"}],"value":"Sulfation on Tyr-21 is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. Tyr-7 and Tyr-12 are sulfated in a sequential manner after Tyr-21 is almost fully sulfated, with the binding affinity for CXCL12/SDF-1alpha increasing with the number of sulfotyrosines present. Sulfotyrosines Tyr-7 and Tyr-12 occupy clefts on opposing CXCL12 subunits, thus bridging the CXCL12 dimer interface and promoting CXCL12 dimerization"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10756055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12034737"}],"value":"O- and N-glycosylated. Asn-11 is the principal site of N-glycosylation. There appears to be very little or no glycosylation on Asn-176. N-glycosylation masks coreceptor function in both X4 and R5 laboratory-adapted and primary HIV-1 strains through inhibiting interaction with their Env glycoproteins. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"WHIM syndrome 1","diseaseAccession":"DI-02419","acronym":"WHIMS1","description":"An autosomal dominant immunologic disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis.","diseaseCrossReference":{"database":"MIM","id":"193670"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12692554"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15536153"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24366360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24553177"}],"value":"CXCR4 mutations play a role in the pathogenesis of Waldenstroem macroglobulinemia (WM) and influence disease presentation and outcome, as well as response to therapy. WM is a B-cell lymphoma characterized by accumulation of malignant lymphoplasmacytic cells in the bone marrow, lymph nodes and spleen, and hypersecretion of monoclonal immunoglobulin M (IgM). Excess IgM production results in serum hyperviscosity, tissue infiltration, and autoimmune-related pathology"}]}},{"texts":[{"value":"Plerixafor (AMD3100), an antagonist of CXCR4 activity, blocks HIV-1 entry, interaction with CXCL12 and subsequent CXCR4 signaling"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00521"}],"value":"Belongs to the G protein-coupled receptor 1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10825158"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12034737"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9427609"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8234909"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8329116"}],"value":"Was originally thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R) (PubMed:8234909, PubMed:8329116). Later reports showed that it acts as a receptor for the C-X-C chemokine CXCL12/SDF-1 (PubMed:10825158, PubMed:12034737, PubMed:9427609)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Miscellaneous discrepancy","sequence":"CAA12166.1","note":"Intron retention.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"CXCR4base","resourceUrl":"https://databases.lovd.nl/shared/genes/CXCR4","ftp":false,"note":"CXCR4 mutation db"},{"commentType":"WEB RESOURCE","resourceName":"Wikipedia","resourceUrl":"https://en.wikipedia.org/wiki/CXC_chemokine_receptors","ftp":false,"note":"CXC chemokine receptors entry"},{"commentType":"WEB RESOURCE","resourceName":"Wikipedia","resourceUrl":"https://en.wikipedia.org/wiki/CXCR4","ftp":false,"note":"CXCR4 entry"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"C-X-C chemokine receptor type 4","featureId":"PRO_0000069352"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Transmembrane","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Topological domain","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Transmembrane","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Topological domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Transmembrane","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Topological domain","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20929726"}]},{"type":"Transmembrane","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Helical; 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