ACKR2_HUMAN
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 03-AUG-2022, entry version 186.
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}.
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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; 9.
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 GlyGen; O00590; 1 site.
DR iPTMnet; O00590; -.
DR PhosphoSitePlus; O00590; -.
DR BioMuta; ACKR2; -.
DR MassIVE; O00590; -.
DR PaxDb; O00590; -.
DR PeptideAtlas; O00590; -.
DR PRIDE; O00590; -.
DR ProteomicsDB; 47990; -.
DR Antibodypedia; 2896; 433 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 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; ENSGT01050000244811; -.
DR InParanoid; O00590; -.
DR OMA; IVHAQPH; -.
DR OrthoDB; 791532at2759; -.
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 1031 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 107 other tissues.
DR ExpressionAtlas; O00590; baseline and differential.
DR Genevisible; O00590; HS.
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:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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 InterPro; IPR033037; Ackr2.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR001277; CXCR4/ACKR2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF735; PTHR10489:SF735; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00645; CXCCHMKINER4.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
