CCRL2_HUMAN
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 03-AUG-2022, entry version 165.
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}.
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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. [O00421-1]
DR RefSeq; XP_016862925.1; XM_017007436.1. [O00421-1]
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 GlyGen; O00421; 1 site.
DR iPTMnet; O00421; -.
DR PhosphoSitePlus; O00421; -.
DR BioMuta; CCRL2; -.
DR jPOST; O00421; -.
DR MassIVE; O00421; -.
DR MaxQB; O00421; -.
DR PaxDb; O00421; -.
DR PeptideAtlas; O00421; -.
DR PRIDE; O00421; -.
DR ProteomicsDB; 47877; -. [O00421-1]
DR ProteomicsDB; 47878; -. [O00421-2]
DR Antibodypedia; 6921; 453 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 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; CKSNYNL; -.
DR OrthoDB; 1277718at2759; -.
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 1069 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 121 other tissues.
DR ExpressionAtlas; O00421; baseline and differential.
DR Genevisible; O00421; HS.
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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
