ID ACKR2_HUMAN Reviewed; 384 AA. AC O00590; B2R8Y8; O00537; Q53YA1; Q86UN9; Q96A02; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2002, sequence version 2. DT 24-JAN-2024, entry version 194. DE RecName: Full=Atypical chemokine receptor 2; DE AltName: Full=C-C chemokine receptor D6; DE AltName: Full=Chemokine receptor CCR-10; DE AltName: Full=Chemokine receptor CCR-9; DE AltName: Full=Chemokine-binding protein 2; DE AltName: Full=Chemokine-binding protein D6; GN Name=ACKR2; Synonyms=CCBP2, CCR10, CMKBR9, D6; 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]. RC TISSUE=Lung; RX PubMed=9364936; DOI=10.1089/dna.1997.16.1249; RA Bonini J.A., Martin S.K., Dralyuk F., Roe M.W., Philipson L.H., RA Steiner D.F.; RT "Cloning, expression, and chromosomal mapping of a novel human CC-chemokine RT receptor (CCR10) that displays high-affinity binding for MCP-1 and MCP-3."; RL DNA Cell Biol. 16:1249-1256(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9405404; DOI=10.1074/jbc.272.51.32078; RA Nibbs R.J.B., Wylie S.M., Yang J., Landau N.R., Graham G.J.; RT "Cloning and characterization of a novel promiscuous human beta-chemokine RT receptor D6."; RL J. Biol. Chem. 272:32078-32083(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-373. RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver, and 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 [7] RP TISSUE SPECIFICITY. RX PubMed=11238036; DOI=10.1016/s0002-9440(10)64035-7; RA Nibbs R.J.B., Kriehuber E., Ponath P.D., Parent D., Qin S., Campbell J.D., RA Henderson A., Kerjaschki D., Maurer D., Graham G.J., Rot A.; RT "The beta-chemokine receptor D6 is expressed by lymphatic endothelium and a RT subset of vascular tumors."; RL Am. J. Pathol. 158:867-877(2001). RN [8] RP C-TERMINAL CYTOPLASMIC TAIL, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=18201974; DOI=10.1074/jbc.m710128200; RA McCulloch C.V., Morrow V., Milasta S., Comerford I., Milligan G., RA Graham G.J., Isaacs N.W., Nibbs R.J.; RT "Multiple roles for the C-terminal tail of the chemokine scavenger D6."; RL J. Biol. Chem. 283:7972-7982(2008). RN [9] RP ERRATUM OF PUBMED:18201974. RA McCulloch C.V., Morrow V., Milasta S., Comerford I., Milligan G., RA Graham G.J., Isaacs N.W., Nibbs R.J.; RL J. Biol. Chem. 288:26820-26820(2013). RN [10] RP REVIEW. RX PubMed=20373092; DOI=10.1007/82_2010_19; RA Bonecchi R., Savino B., Borroni E.M., Mantovani A., Locati M.; RT "Chemokine decoy receptors: structure-function and biological properties."; RL Curr. Top. Microbiol. Immunol. 341:15-36(2010). RN [11] RP TISSUE SPECIFICITY. RX PubMed=22651933; DOI=10.1096/fj.11-194894; RA Pashover-Schallinger E., Aswad M., Schif-Zuck S., Shapiro H., Singer P., RA Ariel A.; RT "The atypical chemokine receptor D6 controls macrophage efferocytosis and RT cytokine secretion during the resolution of inflammation."; RL FASEB J. 26:3891-3900(2012). RN [12] RP REVIEW. RX PubMed=22698181; DOI=10.1016/j.imlet.2012.04.004; RA Graham G.J., Locati M., Mantovani A., Rot A., Thelen M.; RT "The biochemistry and biology of the atypical chemokine receptors."; RL Immunol. Lett. 145:30-38(2012). RN [13] RP REVIEW. RX PubMed=23356288; DOI=10.1042/bst20120246; RA Cancellieri C., Vacchini A., Locati M., Bonecchi R., Borroni E.M.; RT "Atypical chemokine receptors: from silence to sound."; RL Biochem. Soc. Trans. 41:231-236(2013). RN [14] RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=23479571; DOI=10.1182/blood-2012-04-425314; RA McKimmie C.S., Singh M.D., Hewit K., Lopez-Franco O., Le Brocq M., RA Rose-John S., Lee K.M., Baker A.H., Wheat R., Blackbourn D.J., Nibbs R.J., RA Graham G.J.; RT "An analysis of the function and expression of D6 on lymphatic endothelial RT cells."; RL Blood 121:3768-3777(2013). RN [15] RP REVIEW. RX PubMed=23125030; DOI=10.1002/path.4123; RA Graham G.J., Locati M.; RT "Regulation of the immune and inflammatory responses by the 'atypical' RT chemokine receptor D6."; RL J. Pathol. 229:168-175(2013). RN [16] RP REVIEW. RX PubMed=22939232; DOI=10.1016/j.molimm.2012.08.003; RA Cancellieri C., Caronni N., Vacchini A., Savino B., Borroni E.M., RA Locati M., Bonecchi R.; RT "Review: Structure-function and biological properties of the atypical RT chemokine receptor D6."; RL Mol. Immunol. 55:87-93(2013). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23633677; DOI=10.1126/scisignal.2003627; RA Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., RA Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., RA Locati M.; RT "Beta-arrestin-dependent activation of the cofilin pathway is required for RT the scavenging activity of the atypical chemokine receptor D6."; RL Sci. Signal. 6:RA30-RA30(2013). 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 including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CC CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES CC and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta- CC arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway CC that results in the phosphorylation of the actin-binding protein CC cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation CC of this pathway results in up-regulation of ACKR2 from endosomal CC compartment to cell membrane, increasing its efficiency in chemokine CC uptake and degradation. By scavenging chemokines in tissues, on the CC surfaces of lymphatic vessels, and in placenta, plays an essential role CC in the resolution (termination) of the inflammatory response and in the CC regulation of adaptive immune responses. Plays a major role in the CC immune silencing of macrophages during the resolution of inflammation. CC Acts as a regulator of inflammatory leukocyte interactions with CC lymphatic endothelial cells (LECs) and is required for immature/mature CC dendritic cells discrimination by LECs. {ECO:0000269|PubMed:23479571, CC ECO:0000269|PubMed:23633677}. CC -!- INTERACTION: CC O00590; P52803: EFNA5; NbExp=3; IntAct=EBI-13379418, EBI-1753674; CC O00590; P48165: GJA8; NbExp=3; IntAct=EBI-13379418, EBI-17458373; CC O00590; P11836: MS4A1; NbExp=3; IntAct=EBI-13379418, EBI-2808234; CC O00590; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-13379418, EBI-9550165; CC O00590; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-13379418, EBI-3917235; CC O00590; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-13379418, EBI-12808018; CC O00590; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-13379418, EBI-17684533; CC -!- SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cell CC membrane; Multi-pass membrane protein. Note=Predominantly localizes to CC endocytic vesicles, and upon stimulation by the ligand is internalized CC via clathrin-coated pits. Once internalized, the ligand dissociates CC from the receptor, and is targeted to degradation while the receptor is CC recycled back to the cell membrane. CC -!- TISSUE SPECIFICITY: Found in endothelial cells lining afferent CC lymphatics in dermis and lymph nodes. Also found in lymph nodes CC subcapsular and medullary sinuses, tonsillar lymphatic sinuses and CC lymphatics in mucosa and submucosa of small and large intestine and CC appendix. Also found in some malignant vascular tumors. Expressed at CC high levels in Kaposi sarcoma-related pathologies. Expressed on CC apoptotic neutrophils (at protein level). Expressed primarily in CC placenta and fetal liver, and found at very low levels in the lung and CC lymph node. {ECO:0000269|PubMed:11238036, ECO:0000269|PubMed:22651933, CC ECO:0000269|PubMed:23479571}. CC -!- INDUCTION: By interleukin-6 and interferon-gamma. CC {ECO:0000269|PubMed:23479571}. CC -!- DOMAIN: The C-terminal cytoplasmic tail controls its phosphorylation, CC stability, intracellular trafficking itinerary, and chemokine CC scavenging properties. CC -!- PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic CC tail. {ECO:0000269|PubMed:18201974}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00521}. 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; U94888; AAB97728.1; -; mRNA. DR EMBL; Y12815; CAA73346.1; -; mRNA. DR EMBL; AY262687; AAP20651.1; -; Genomic_DNA. DR EMBL; BT006800; AAP35446.1; -; mRNA. DR EMBL; AK313561; BAG36335.1; -; mRNA. DR EMBL; BC008816; AAH08816.1; -; mRNA. DR EMBL; BC011631; AAH11631.1; -; mRNA. DR EMBL; BC020558; AAH20558.1; -; mRNA. DR EMBL; BC101629; AAI01630.1; -; mRNA. DR EMBL; BC112045; AAI12046.1; -; mRNA. DR CCDS; CCDS2706.1; -. DR RefSeq; NP_001287.2; NM_001296.4. DR AlphaFoldDB; O00590; -. DR SMR; O00590; -. DR BioGRID; 107643; 88. DR IntAct; O00590; 8. DR STRING; 9606.ENSP00000416996; -. DR BindingDB; O00590; -. DR ChEMBL; CHEMBL4105988; -. DR TCDB; 9.A.14.13.35; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; O00590; 1 site, No reported glycans. DR GlyGen; O00590; 1 site. DR iPTMnet; O00590; -. DR PhosphoSitePlus; O00590; -. DR BioMuta; ACKR2; -. DR MassIVE; O00590; -. DR PaxDb; 9606-ENSP00000416996; -. DR PeptideAtlas; O00590; -. DR ProteomicsDB; 47990; -. DR Antibodypedia; 2896; 478 antibodies from 36 providers. DR DNASU; 1238; -. DR Ensembl; ENST00000422265.6; ENSP00000416996.1; ENSG00000144648.16. DR Ensembl; ENST00000442925.5; ENSP00000396150.1; ENSG00000144648.16. DR GeneID; 1238; -. DR KEGG; hsa:1238; -. DR MANE-Select; ENST00000422265.6; ENSP00000416996.1; NM_001296.5; NP_001287.2. DR UCSC; uc003cme.4; human. DR AGR; HGNC:1565; -. DR CTD; 1238; -. DR DisGeNET; 1238; -. DR GeneCards; ACKR2; -. DR HGNC; HGNC:1565; ACKR2. DR HPA; ENSG00000144648; Tissue enhanced (liver, placenta). DR MIM; 602648; gene. DR neXtProt; NX_O00590; -. DR OpenTargets; ENSG00000144648; -. DR PharmGKB; PA26139; -. DR VEuPathDB; HostDB:ENSG00000144648; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230359; -. DR InParanoid; O00590; -. DR OMA; IVHAQPH; -. DR OrthoDB; 5350443at2759; -. DR PhylomeDB; O00590; -. DR TreeFam; TF330966; -. DR PathwayCommons; O00590; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR SignaLink; O00590; -. DR BioGRID-ORCS; 1238; 13 hits in 1107 CRISPR screens. DR ChiTaRS; ACKR2; human. DR GeneWiki; CCBP2; -. DR GenomeRNAi; 1238; -. DR Pharos; O00590; Tbio. DR PRO; PR:O00590; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O00590; Protein. DR Bgee; ENSG00000144648; Expressed in placenta and 108 other cell types or tissues. DR ExpressionAtlas; O00590; baseline and differential. DR GO; GO:0005884; C:actin filament; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA: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:0004950; F:chemokine receptor activity; IDA:ProtInc. DR GO; GO:0005044; F:scavenger receptor activity; IMP:UniProtKB. DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR CDD; cd15188; 7tmA_ACKR2_D6; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR001277; CXCR4/ACKR2. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF942; ATYPICAL CHEMOKINE RECEPTOR 2; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. DR PRINTS; PR00645; CXCCHMKINER4. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; O00590; HS. PE 1: Evidence at protein level; KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor; KW Glycoprotein; Inflammatory response; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..384 FT /note="Atypical chemokine receptor 2" FT /id="PRO_0000069219" FT TOPO_DOM 1..50 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 51..71 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 72..92 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 93..113 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 114..118 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 119..140 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 141..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..217 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 239..250 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 251..271 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 272..293 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 294..314 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 315..384 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 327..384 FT /note="C-terminal cytoplasmic tail" FT REGION 363..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 19 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 117..195 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VARIANT 41 FT /note="V -> A (in dbSNP:rs2228467)" FT /id="VAR_049379" FT VARIANT 248 FT /note="A -> V (in dbSNP:rs2228469)" FT /id="VAR_049380" FT VARIANT 311 FT /note="L -> V (in dbSNP:rs6779520)" FT /id="VAR_049381" FT VARIANT 373 FT /note="Y -> S (in dbSNP:rs2228468)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_024252" FT CONFLICT 17 FT /note="S -> A (in Ref. 1; AAB97728)" FT /evidence="ECO:0000305" FT CONFLICT 161 FT /note="S -> N (in Ref. 1; AAB97728)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="Q -> L (in Ref. 1; AAB97728)" FT /evidence="ECO:0000305" SQ SEQUENCE 384 AA; 43443 MW; 464C5703C1DE9A6A CRC64; MAATASPQPL ATEDADSENS SFYYYDYLDE VAFMLCRKDA VVSFGKVFLP VFYSLIFVLG LSGNLLLLMV LLRYVPRRRM VEIYLLNLAI SNLLFLVTLP FWGISVAWHW VFGSFLCKMV STLYTINFYS GIFFISCMSL DKYLEIVHAQ PYHRLRTRAK SLLLATIVWA VSLAVSIPDM VFVQTHENPK GVWNCHADFG GHGTIWKLFL RFQQNLLGFL LPLLAMIFFY SRIGCVLVRL RPAGQGRALK IAAALVVAFF VLWFPYNLTL FLHTLLDLQV FGNCEVSQHL DYALQVTESI AFLHCCFSPI LYAFSSHRFR QYLKAFLAAV LGWHLAPGTA QASLSSCSES SILTAQEEMT GMNDLGERQS ENYPNKEDVG NKSA //