ID CCRL2_HUMAN Reviewed; 344 AA. AC O00421; B4DKQ8; O75307; Q4VBB0; Q6IPX0; Q7KYQ9; Q96KP5; Q9UPG0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 24-JAN-2024, entry version 173. DE RecName: Full=C-C chemokine receptor-like 2; DE AltName: Full=Chemokine receptor CCR11; DE AltName: Full=Chemokine receptor X; DE AltName: Full=Putative MCP-1 chemokine receptor; GN Name=CCRL2; Synonyms=CCR11, CCR6, CKRX, CRAM, HCR; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP TYR-167. RX PubMed=9473515; DOI=10.1006/bbrc.1997.7981; RA Fan P., Kyaw H., Su K., Zeng Z., Augustus M., Carter K.C., Li Y.; RT "Cloning and characterization of a novel human chemokine receptor."; RL Biochem. Biophys. Res. Commun. 243:264-268(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-167. RC TISSUE=Leukocyte; RA Ansari-Lari M.A., Liu X.-M., Gorrell J.H., Gibbs R.A.; RT "Haplotype analysis of a gene cluster containing CCR5 and a new member of RT chemokine receptor gene family."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-243. RC TISSUE=Monocyte; RA Gish K., McClanahan T.K., Moore K.W.; RT "CRAM: a novel human chemokine receptor-like gene expressed in activated RT monocytes."; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Microglia; RA Biber K.P.H.; RT "Cloning and characterisation of a new MCP-1 chemokine receptor CCR11."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Umbilical cord blood; 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] (ISOFORM 1), AND VARIANT TYR-167. RC TISSUE=Lung; 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 (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-167. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS TYR-167 RP AND MET-168. RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis; 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 [9] RP TISSUE SPECIFICITY. RX PubMed=11828366; RX DOI=10.1002/1521-4141(200202)32:2<494::aid-immu494>3.0.co;2-y; RA Migeotte I., Franssen J.D., Goriely S., Willems F., Parmentier M.; RT "Distribution and regulation of expression of the putative human chemokine RT receptor HCR in leukocyte populations."; RL Eur. J. Immunol. 32:494-501(2002). RN [10] RP TISSUE SPECIFICITY, AND LACK OF RESPOND BY CCL2. RX PubMed=15188357; DOI=10.1002/art.20275; RA Galligan C.L., Matsuyama W., Matsukawa A., Mizuta H., Hodge D.R., RA Howard O.M., Yoshimura T.; RT "Up-regulated expression and activation of the orphan chemokine receptor, RT CCRL2, in rheumatoid arthritis."; RL Arthritis Rheum. 50:1806-1814(2004). RN [11] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=18397265; DOI=10.1111/j.1365-2567.2008.02836.x; RA Hartmann T.N., Leick M., Ewers S., Diefenbacher A., Schraufstatter I., RA Honczarenko M., Burger M.; RT "Human B cells express the orphan chemokine receptor CRAM-A/B in a RT maturation-stage-dependent and CCL5-modulated manner."; RL Immunology 125:252-262(2008). RN [12] RP SUBCELLULAR LOCATION, AND LIGAND-BINDING. RX PubMed=20002784; DOI=10.1111/j.1365-2567.2009.03209.x; RA Leick M., Catusse J., Follo M., Nibbs R.J., Hartmann T.N., Veelken H., RA Burger M.; RT "CCL19 is a specific ligand of the constitutively recycling atypical human RT chemokine receptor CRAM-B."; RL Immunology 129:536-546(2010). CC -!- FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to CC be a signaling receptor, but may have a role in modulating chemokine- CC triggered immune responses by capturing and internalizing CCL19 or by CC presenting RARRES2 ligand to CMKLR1, a functional signaling receptors. CC Plays a critical role for the development of Th2 responses. CC -!- INTERACTION: CC O00421-2; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-12874086, EBI-12003442; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18397265, CC ECO:0000269|PubMed:20002784}; Multi-pass membrane protein CC {ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:20002784}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=CRAM-B; CC IsoId=O00421-1; Sequence=Displayed; CC Name=2; Synonyms=CRAM-A; CC IsoId=O00421-2; Sequence=VSP_018584; CC -!- TISSUE SPECIFICITY: Expressed abundantly in immunal tissues such as CC spleen, fetal liver, lymph node and bone marrow. Strong expression also CC in lung and heart. Expressed in almost all hematopoietic cells CC including monocytes, macrophages, PMNs, T-cells (both CD4+ and CD8+), CC monocyte-derived iDCs, NK cells, and CD34+ progenitor cells. B-cells CC expressed isoform 1 but not isoform 2. Up-regulated on synovial CC neutrophils of rheumatoid arthritis patients. CC {ECO:0000269|PubMed:11828366, ECO:0000269|PubMed:15188357, CC ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:9473515}. CC -!- INDUCTION: Up-regulated by CCL5 on the pre-B-cell lines NALM-6 and G2. CC {ECO:0000269|PubMed:18397265}. CC -!- DOMAIN: Lacks the conserved DRYLAIV motif in the second intracellular CC loop that is required for signaling of functional chemokine receptors. CC -!- MISCELLANEOUS: It was initially reported that CCRL2 responds CC functionally to CCL2, CCL5, CCL7, and CCL8 via intracellular calcium CC mobilization and transwell chemotaxis although no evidence for a direct CC ligand-receptor interaction was provided in this report. These results CC are now controversial, and other studies failed to confirm CCRL2 CC recognition and transwell chemotaxis of these chemokines or a series of CC other CC- and CXC-chemokines using CCRL2-transfected cells CC (PubMed:15188357). {ECO:0000305|PubMed:15188357}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-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; U97123; AAC39595.1; -; mRNA. DR EMBL; AF014958; AAB82106.1; -; mRNA. DR EMBL; AF015524; AAC34601.1; -; mRNA. DR EMBL; AF015525; AAC34602.1; -; mRNA. DR EMBL; AJ344142; CAC82985.1; -; mRNA. DR EMBL; AK296673; BAG59270.1; -; mRNA. DR EMBL; AY337001; AAQ76789.1; -; mRNA. DR EMBL; U95626; AAB57794.1; -; Genomic_DNA. DR EMBL; BC025717; AAH25717.1; -; mRNA. DR EMBL; BC071682; AAH71682.1; -; mRNA. DR EMBL; BC096075; AAH96075.1; -; mRNA. DR EMBL; BC096076; AAH96076.1; -; mRNA. DR EMBL; BC099623; AAH99623.1; -; mRNA. DR CCDS; CCDS43079.1; -. [O00421-1] DR CCDS; CCDS46814.1; -. [O00421-2] DR PIR; JC5942; JC5942. DR RefSeq; NP_001124382.1; NM_001130910.1. [O00421-2] DR RefSeq; NP_003956.2; NM_003965.4. [O00421-1] DR RefSeq; XP_011532510.1; XM_011534208.1. [O00421-1] DR RefSeq; XP_011532511.1; XM_011534209.1. DR RefSeq; XP_016862925.1; XM_017007436.1. DR AlphaFoldDB; O00421; -. DR SMR; O00421; -. DR BioGRID; 114500; 19. DR IntAct; O00421; 6. DR STRING; 9606.ENSP00000349967; -. DR BindingDB; O00421; -. DR ChEMBL; CHEMBL2321627; -. DR GuidetoPHARMACOLOGY; 78; -. DR GlyCosmos; O00421; 1 site, No reported glycans. DR GlyGen; O00421; 1 site. DR iPTMnet; O00421; -. DR PhosphoSitePlus; O00421; -. DR SwissPalm; O00421; -. DR BioMuta; CCRL2; -. DR jPOST; O00421; -. DR MassIVE; O00421; -. DR MaxQB; O00421; -. DR PaxDb; 9606-ENSP00000349967; -. DR PeptideAtlas; O00421; -. DR ProteomicsDB; 47877; -. [O00421-1] DR ProteomicsDB; 47878; -. [O00421-2] DR Antibodypedia; 6921; 473 antibodies from 34 providers. DR DNASU; 9034; -. DR Ensembl; ENST00000357392.4; ENSP00000349967.4; ENSG00000121797.10. [O00421-2] DR Ensembl; ENST00000399036.4; ENSP00000381994.3; ENSG00000121797.10. [O00421-1] DR Ensembl; ENST00000400880.3; ENSP00000383677.3; ENSG00000121797.10. [O00421-1] DR Ensembl; ENST00000400882.2; ENSP00000383678.2; ENSG00000121797.10. [O00421-1] DR GeneID; 9034; -. DR KEGG; hsa:9034; -. DR MANE-Select; ENST00000399036.4; ENSP00000381994.3; NM_003965.5; NP_003956.2. DR UCSC; uc003cpp.5; human. [O00421-1] DR AGR; HGNC:1612; -. DR CTD; 9034; -. DR DisGeNET; 9034; -. DR GeneCards; CCRL2; -. DR HGNC; HGNC:1612; CCRL2. DR HPA; ENSG00000121797; Low tissue specificity. DR MIM; 608379; gene. DR neXtProt; NX_O00421; -. DR OpenTargets; ENSG00000121797; -. DR PharmGKB; PA26175; -. DR VEuPathDB; HostDB:ENSG00000121797; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230359; -. DR InParanoid; O00421; -. DR OMA; FYKPQME; -. DR OrthoDB; 5265544at2759; -. DR PhylomeDB; O00421; -. DR TreeFam; TF330966; -. DR PathwayCommons; O00421; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR SignaLink; O00421; -. DR BioGRID-ORCS; 9034; 28 hits in 1150 CRISPR screens. DR GeneWiki; CCRL2; -. DR GenomeRNAi; 9034; -. DR Pharos; O00421; Tchem. DR PRO; PR:O00421; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O00421; Protein. DR Bgee; ENSG00000121797; Expressed in mucosa of transverse colon and 122 other cell types or tissues. DR ExpressionAtlas; O00421; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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:0048020; F:CCR chemokine receptor binding; IPI:UniProtKB. DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc. DR GO; GO:0042379; F:chemokine receptor binding; IPI: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:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR CDD; cd15171; 7tmA_CCRL2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF655; C-C CHEMOKINE RECEPTOR-LIKE 2; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. 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; O00421; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..344 FT /note="C-C chemokine receptor-like 2" FT /id="PRO_0000236798" FT TOPO_DOM 1..43 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 44..64 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 65..74 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 75..95 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 96..104 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 105..125 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 126..144 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 145..165 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 166..198 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 220..238 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 239..259 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 260..286 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 287..307 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 308..344 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 324..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 3 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 103..181 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 1 FT /note="M -> MIYTRFLKGSLKM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_018584" FT VARIANT 4 FT /note="Y -> C (in dbSNP:rs11574443)" FT /id="VAR_049385" FT VARIANT 167 FT /note="F -> Y (in dbSNP:rs3204849)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16641997, ECO:0000269|PubMed:9473515, FT ECO:0000269|Ref.2, ECO:0000269|Ref.6" FT /id="VAR_026488" FT VARIANT 168 FT /note="V -> M (in dbSNP:rs6441977)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_026489" FT VARIANT 243 FT /note="I -> V (in dbSNP:rs3204850)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_026490" FT CONFLICT 45 FT /note="C -> S (in Ref. 5; BAG59270)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="K -> R (in Ref. 5; BAG59270)" FT /evidence="ECO:0000305" FT CONFLICT 158 FT /note="T -> Q (in Ref. 4; CAC82985)" FT /evidence="ECO:0000305" FT CONFLICT 334 FT /note="S -> P (in Ref. 5; BAG59270)" FT /evidence="ECO:0000305" SQ SEQUENCE 344 AA; 39513 MW; D8BBF3A0EE5BB14C CRC64; MANYTLAPED EYDVLIEGEL ESDEAEQCDK YDAQALSAQL VPSLCSAVFV IGVLDNLLVV LILVKYKGLK RVENIYLLNL AVSNLCFLLT LPFWAHAGGD PMCKILIGLY FVGLYSETFF NCLLTVQRYL VFLHKGNFFS ARRRVPCGII TSVLAWVTAI LATLPEFVVY KPQMEDQKYK CAFSRTPFLP ADETFWKHFL TLKMNISVLV LPLFIFTFLY VQMRKTLRFR EQRYSLFKLV FAIMVVFLLM WAPYNIAFFL STFKEHFSLS DCKSSYNLDK SVHITKLIAT THCCINPLLY AFLDGTFSKY LCRCFHLRSN TPLQPRGQSA QGTSREEPDH STEV //