ACKR3_MOUSE
ID ACKR3_MOUSE Reviewed; 362 AA.
AC P56485; Q91WI0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Atypical chemokine receptor 3 {ECO:0000305};
DE AltName: Full=C-X-C chemokine receptor type 7;
DE Short=CXC-R7;
DE Short=CXCR-7;
DE AltName: Full=Chemokine orphan receptor 1;
DE AltName: Full=G-protein coupled receptor RDC1 homolog;
DE Short=RDC-1;
GN Name=Ackr3 {ECO:0000312|MGI:MGI:109562}; Synonyms=Cmkor1, Cxcr7, Rdc1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Peritoneal exudate;
RX PubMed=9510554; DOI=10.1007/s002510050371;
RA Heesen M., Berman M.A., Charest A., Housman D., Gerard C., Dorf M.E.;
RT "Cloning and chromosomal mapping of an orphan chemokine receptor: mouse
RT RDC1.";
RL Immunogenetics 47:364-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16940167; DOI=10.1084/jem.20052144;
RA Burns J.M., Summers B.C., Wang Y., Melikian A., Berahovich R., Miao Z.,
RA Penfold M.E., Sunshine M.J., Littman D.R., Kuo C.J., Wei K., McMaster B.E.,
RA Wright K., Howard M.C., Schall T.J.;
RT "A novel chemokine receptor for SDF-1 and I-TAC involved in cell survival,
RT cell adhesion, and tumor development.";
RL J. Exp. Med. 203:2201-2213(2006).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17804806; DOI=10.1073/pnas.0702229104;
RA Sierro F., Biben C., Martinez-Munoz L., Mellado M., Ransohoff R.M., Li M.,
RA Woehl B., Leung H., Groom J., Batten M., Harvey R.P., Martinez-A C.,
RA Mackay C.R., Mackay F.;
RT "Disrupted cardiac development but normal hematopoiesis in mice deficient
RT in the second CXCL12/SDF-1 receptor, CXCR7.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14759-14764(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18442043; DOI=10.1002/dvg.20387;
RA Gerrits H., van Ingen Schenau D.S., Bakker N.E., van Disseldorp A.J.,
RA Strik A., Hermens L.S., Koenen T.B., Krajnc-Franken M.A., Gossen J.A.;
RT "Early postnatal lethality and cardiovascular defects in CXCR7-deficient
RT mice.";
RL Genesis 46:235-245(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-350 AND SER-355, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=20681075; DOI=10.1016/j.jneuroim.2010.05.011;
RA Tiveron M.C., Boutin C., Daou P., Moepps B., Cremer H.;
RT "Expression and function of CXCR7 in the mouse forebrain.";
RL J. Neuroimmunol. 224:72-79(2010).
RN [9]
RP FUNCTION.
RX PubMed=20161793; DOI=10.1371/journal.pone.0009175;
RA Naumann U., Cameroni E., Pruenster M., Mahabaleshwar H., Raz E.,
RA Zerwes H.G., Rot A., Thelen M.;
RT "CXCR7 functions as a scavenger for CXCL12 and CXCL11.";
RL PLoS ONE 5:E9175-E9175(2010).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21246655; DOI=10.1002/dvdy.22549;
RA Yu S., Crawford D., Tsuchihashi T., Behrens T.W., Srivastava D.;
RT "The chemokine receptor CXCR7 functions to regulate cardiac valve
RT remodeling.";
RL Dev. Dyn. 240:384-393(2011).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21220100; DOI=10.1016/j.neuron.2010.12.006;
RA Sanchez-Alcaniz J.A., Haege S., Mueller W., Pla R., Mackay F., Schulz S.,
RA Lopez-Bendito G., Stumm R., Marin O.;
RT "Cxcr7 controls neuronal migration by regulating chemokine
RT responsiveness.";
RL Neuron 69:77-90(2011).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=31211835; DOI=10.1093/hmg/ddz137;
RA Whitman M.C., Miyake N., Nguyen E.H., Bell J.L., Matos Ruiz P.M.,
RA Chan W.M., Di Gioia S.A., Mukherjee N., Barry B.J., Bosley T.M., Khan A.O.,
RA Engle E.C.;
RT "Decreased ACKR3 (CXCR7) function causes oculomotor synkinesis in mice and
RT humans.";
RL Hum. Mol. Genet. 28:3113-3125(2019).
CC -!- FUNCTION: Atypical chemokine receptor that controls chemokine levels
CC and localization via high-affinity chemokine binding that is uncoupled
CC from classic ligand-driven signal transduction cascades, resulting
CC instead in chemokine sequestration, degradation, or transcytosis. Also
CC known as interceptor (internalizing receptor) or chemokine-scavenging
CC receptor or chemokine decoy receptor. Acts as a receptor for chemokines
CC CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-
CC mediated signal transduction but instead induces beta-arrestin
CC recruitment, leading to ligand internalization and activation of MAPK
CC signaling pathway. Required for regulation of CXCR4 protein levels in
CC migrating interneurons, thereby adapting their chemokine
CC responsiveness. In glioma cells, transduces signals via MEK/ERK
CC pathway, mediating resistance to apoptosis. Promotes cell growth and
CC survival. Not involved in cell migration, adhesion or proliferation of
CC normal hematopoietic progenitors but activated by CXCL11 in malignant
CC hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1)
CC and enhanced cell adhesion and migration. Plays a regulatory role in
CC CXCR4-mediated activation of cell surface integrins by CXCL12. Required
CC for heart valve development. Regulates axon guidance in the oculomotor
CC system through the regulation of CXCL12 levels (PubMed:31211835).
CC {ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:18442043,
CC ECO:0000269|PubMed:20161793, ECO:0000269|PubMed:21220100,
CC ECO:0000269|PubMed:21246655, ECO:0000269|PubMed:31211835}.
CC -!- SUBUNIT: Homodimer. Can form heterodimers with CXCR4;
CC heterodimerization may regulate CXCR4 signaling activity. Interacts
CC with ARRB1 and ARRB2. {ECO:0000250|UniProtKB:P25106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21220100};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21220100}. Early
CC endosome {ECO:0000250|UniProtKB:P25106}. Recycling endosome
CC {ECO:0000269|PubMed:21220100}. Note=Predominantly localizes to
CC endocytic vesicles, and upon stimulation by the ligand is internalized
CC via clathrin-coated pits in a beta-arrestin-dependent manner. Once
CC internalized, the ligand dissociates from the receptor, and is targeted
CC to degradation while the receptor is recycled back to the cell
CC membrane. {ECO:0000250|UniProtKB:P25106}.
CC -!- TISSUE SPECIFICITY: Not detected in blood, liver, lung and heart, but
CC high expression detected in several tumor cell lines (at protein
CC level). Expressed in heart, spleen, kidney, lung, ovary, brain, testis,
CC astrocytes, neutrophils and B-lymphocytes.
CC {ECO:0000269|PubMed:16940167, ECO:0000269|PubMed:17804806,
CC ECO:0000269|PubMed:9510554}.
CC -!- DEVELOPMENTAL STAGE: Expression detected after 9.5 dpc in the
CC endothelial layer of the forming heart, neural tube, brain and septum
CC transversum. At 10.5 dpc, expressed at high levels in the
CC prosencephalon and in a part of the rhombencephalon and at lower levels
CC in the neural tube, somites and heart. Detected in liver at 11 dpc and
CC 13 dpc, but not at 15 dpc and 17 dpc. During heart development,
CC expression detected mainly in endocardial cells and endocardial cushion
CC mesenchymal cells in both outflow tract and atrioventricular canal
CC regions and to a lesser degree in myocardial cells at 10.5 dpc, in the
CC mesenchyme of the forming valves and in numerous microvessels in the
CC myocardium at 12.5 dpc, and from 14.5 dpc onward mainly in the
CC microvasculature associated with myocardium, valves and great vessels.
CC In developing telencephalon, observed at 11.5 dpc in the ventral
CC telencephalon in proliferative zones of the medial ganglionic eminence
CC (MGE), in ventral part of the lateral ganglionic eminence (LGE) and in
CC Cajal-Retzius (CR) neurons of dorsal telencephalon. At 12.5 dpc,
CC detected in migrating olfactory tubercle neuron precursors and cortical
CC interneurons, and in CR cells and subplate neurons of the cortex. At
CC 13.5 dpc, observed in the germinal zone of MGE in the subpallium, in
CC the marginal zone and cortical subventricular zone (SVZ) of the lateral
CC cortex as well as in pyramidal cells and tangentially migrating
CC interneurons. At postnatal stages, expressed in postnatal cortical
CC plate and in migrating olfactory bulb interneurons in the striatal SVZ
CC and rostral migratory stream. Expressed in the developing
CC neuroepithelium in the region of the developing oculomotor nucleus at
CC 11.5 dpc and 13.5 dpc (PubMed:31211835). {ECO:0000269|PubMed:16940167,
CC ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:20681075,
CC ECO:0000269|PubMed:21220100, ECO:0000269|PubMed:21246655,
CC ECO:0000269|PubMed:31211835}.
CC -!- DOMAIN: The C-terminal cytoplasmic tail, plays a key role in: correct
CC trafficking to the cell membrane, recruitment of beta-arrestin,
CC ubiquitination, and in chemokine scavenging and signaling functions.
CC The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic
CC tail are essential for beta-arrestin recruitment and ubiquitination
CC respectively. {ECO:0000250|UniProtKB:P25106}.
CC -!- PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may be
CC phosphorylated. {ECO:0000250|UniProtKB:P25106}.
CC -!- PTM: Ubiquitinated at the Lys residues in its C-terminal cytoplasmic
CC tail and is essential for correct trafficking from and to the cell
CC membrane. Deubiquitinated by CXCL12-stimulation in a reversible manner.
CC {ECO:0000250|UniProtKB:P25106}.
CC -!- DISRUPTION PHENOTYPE: Lethal at perinatal stages, with most of the
CC neonates dying within 24 hours. Mutants display slightly enlarged
CC heart, but no clear effect on heart functionality is observed. Mutant
CC mice display abnormalities in semilunar valves and ventricles,
CC myocardial degeneration and fibrosis, as well as abnormal intracortical
CC migration of interneurons and premature invasion of the cortical plate.
CC According to PubMed:17804806, mutants display ventricular septal and
CC atrial septal defects. According to PubMed:21246655, mutants display
CC ventricular septal defects but no atrial septal defects. According to
CC PubMed:18442043, no abnormalities in semilunar valve formation or
CC ventricular septal defects are observed. No effect on hematopoiesis,
CC neural development and gastrointestinal vascularization is observed. No
CC apparent bone phenotype is observed. Mutant embryos show oculomotor
CC nerve misrouting, ranging from complete misprojection in the midbrain,
CC to aberrant peripheral branching, to a thin nerve, which aberrantly
CC innervates the lateral rectus (PubMed:31211835).
CC {ECO:0000269|PubMed:17804806, ECO:0000269|PubMed:18442043,
CC ECO:0000269|PubMed:21220100, ECO:0000269|PubMed:21246655,
CC ECO:0000269|PubMed:31211835}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
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DR EMBL; AF000236; AAB71343.1; -; mRNA.
DR EMBL; AK031100; BAC27252.1; -; mRNA.
DR EMBL; BC015254; AAH15254.1; -; mRNA.
DR CCDS; CCDS15152.1; -.
DR RefSeq; NP_001258536.1; NM_001271607.1.
DR RefSeq; NP_031748.2; NM_007722.4.
DR AlphaFoldDB; P56485; -.
DR SMR; P56485; -.
DR IntAct; P56485; 1.
DR STRING; 10090.ENSMUSP00000069114; -.
DR BindingDB; P56485; -.
DR ChEMBL; CHEMBL4105796; -.
DR GlyGen; P56485; 2 sites.
DR iPTMnet; P56485; -.
DR PhosphoSitePlus; P56485; -.
DR jPOST; P56485; -.
DR MaxQB; P56485; -.
DR PaxDb; P56485; -.
DR PRIDE; P56485; -.
DR ProteomicsDB; 285935; -.
DR ABCD; P56485; 1 sequenced antibody.
DR Antibodypedia; 47699; 824 antibodies from 39 providers.
DR DNASU; 12778; -.
DR Ensembl; ENSMUST00000065587; ENSMUSP00000069114; ENSMUSG00000044337.
DR GeneID; 12778; -.
DR KEGG; mmu:12778; -.
DR UCSC; uc007bzh.2; mouse.
DR CTD; 57007; -.
DR MGI; MGI:109562; Ackr3.
DR VEuPathDB; HostDB:ENSMUSG00000044337; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244811; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P56485; -.
DR OMA; HFIPFSC; -.
DR OrthoDB; 819032at2759; -.
DR PhylomeDB; P56485; -.
DR TreeFam; TF333489; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 12778; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ackr3; mouse.
DR PRO; PR:P56485; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P56485; protein.
DR Bgee; ENSMUSG00000044337; Expressed in metanephric cortical collecting duct and 264 other tissues.
DR Genevisible; P56485; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0019958; F:C-X-C chemokine binding; ISS:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0021557; P:oculomotor nerve development; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:1905322; P:positive regulation of mesenchymal stem cell migration; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:InterPro.
DR InterPro; IPR001416; ACKR3.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF931; PTHR10489:SF931; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00646; RDC1ORPHANR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Developmental protein; Disulfide bond;
KW Endosome; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..362
FT /note="Atypical chemokine receptor 3"
FT /id="PRO_0000070102"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 324..362
FT /note="C-terminal cytoplasmic tail"
FT /evidence="ECO:0000250"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 97
FT /note="I -> T (in Ref. 1; AAB71343)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="T -> A (in Ref. 1; AAB71343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41636 MW; 7A0399DED5B73E66 CRC64;
MDVHLFDYAE PGNYSDINWP CNSSDCIVVD TVQCPTMPNK NVLLYTLSFI YIFIFVIGMI
ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVITIPVW VVSLVQHNQW PMGELTCKIT
HLIFSINLFG SIFFLACMSV DRYLSITYFT GTSSYKKKMV RRVVCILVWL LAFFVSLPDT
YYLKTVTSAS NNETYCRSFY PEHSIKEWLI GMELVSVILG FAVPFTIIAI FYFLLARAMS
ASGDQEKHSS RKIIFSYVVV FLVCWLPYHF VVLLDIFSIL HYIPFTCQLE NVLFTALHVT
QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQN
TK
