GPR61_HUMAN
ID GPR61_HUMAN Reviewed; 451 AA.
AC Q9BZJ8; A8K1W2; Q6NWS0; Q8TDV4; Q96PR4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=G-protein coupled receptor 61 {ECO:0000305};
DE AltName: Full=Biogenic amine receptor-like G-protein coupled receptor {ECO:0000303|PubMed:11690637};
GN Name=GPR61; Synonyms=BALGR {ECO:0000303|PubMed:11690637}, GPCR3;
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].
RX PubMed=11165367; DOI=10.1016/s0169-328x(00)00242-4;
RA Lee D.K., George S.R., Cheng R., Nguyen T., Liu Y., Brown M., Lynch K.R.,
RA O'Dowd B.F.;
RT "Identification of four novel human G protein-coupled receptors expressed
RT in the brain.";
RL Brain Res. Mol. Brain Res. 86:13-22(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=11690637; DOI=10.1016/s0167-4781(01)00289-5;
RA Cikos S., Gregor P., Koppel J.;
RT "Cloning of a novel biogenic amine receptor-like G protein-coupled receptor
RT expressed in human brain.";
RL Biochim. Biophys. Acta 1521:66-72(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT "Identification of G protein-coupled receptor genes from the human genome
RT sequence.";
RL FEBS Lett. 520:97-101(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP GLYCOSYLATION AT ASN-12, MUTAGENESIS OF ASN-12, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29226084; DOI=10.1002/2211-5463.12339;
RA Kozielewicz P., Alomar H., Yusof S., Grafton G., Cooper A.J., Curnow S.J.,
RA Ironside J.W., Pall H., Barnes N.M.;
RT "N-glycosylation and expression in human tissues of the orphan GPR61
RT receptor.";
RL FEBS Open Bio 7:1982-1993(2017).
RN [9]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH MTNR1B, FUNCTION, AND
RP INTERACTION WITH ARRB1 AND ARRB2.
RX PubMed=28827538; DOI=10.1038/s41598-017-08996-7;
RA Oishi A., Karamitri A., Gerbier R., Lahuna O., Ahmad R., Jockers R.;
RT "Orphan GPR61, GPR62 and GPR135 receptors and the melatonin MT2 receptor
RT reciprocally modulate their signaling functions.";
RL Sci. Rep. 7:8990-8990(2017).
CC -!- FUNCTION: Orphan G-protein coupled receptor. Constitutively activates
CC the G(s)-alpha/cAMP signaling pathway (PubMed:28827538). Shows a
CC reciprocal regulatory interaction with the melatonin receptor MTNR1B
CC most likely through receptor heteromerization (PubMed:28827538). May be
CC involved in the regulation of food intake and body weight (By
CC similarity). {ECO:0000250|UniProtKB:Q8C010,
CC ECO:0000269|PubMed:28827538}.
CC -!- SUBUNIT: Forms heterodimer with MTNR1B (PubMed:28827538). Interacts
CC with ARRB1 and ARRB2 in a spontaneous and agonist-independent manner;
CC leading to the internalization of GPR61 in the endosomal compartment
CC (PubMed:28827538). {ECO:0000269|PubMed:28827538}.
CC -!- INTERACTION:
CC Q9BZJ8; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-12808020, EBI-2808844;
CC Q9BZJ8; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-12808020, EBI-3904417;
CC Q9BZJ8; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-12808020, EBI-12003442;
CC Q9BZJ8; Q9NY35: CLDND1; NbExp=3; IntAct=EBI-12808020, EBI-4319704;
CC Q9BZJ8; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-12808020, EBI-12019274;
CC Q9BZJ8; P54852: EMP3; NbExp=3; IntAct=EBI-12808020, EBI-3907816;
CC Q9BZJ8; P48165: GJA8; NbExp=3; IntAct=EBI-12808020, EBI-17458373;
CC Q9BZJ8; O95452: GJB6; NbExp=3; IntAct=EBI-12808020, EBI-13345609;
CC Q9BZJ8; P26715: KLRC1; NbExp=3; IntAct=EBI-12808020, EBI-9018187;
CC Q9BZJ8; P60201-2: PLP1; NbExp=3; IntAct=EBI-12808020, EBI-12188331;
CC Q9BZJ8; Q01453: PMP22; NbExp=3; IntAct=EBI-12808020, EBI-2845982;
CC Q9BZJ8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12808020, EBI-17247926;
CC Q9BZJ8; Q9Y666-2: SLC12A7; NbExp=3; IntAct=EBI-12808020, EBI-12854384;
CC Q9BZJ8; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-12808020, EBI-12808018;
CC Q9BZJ8; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-12808020, EBI-12266234;
CC Q9BZJ8; P0DN84: STRIT1; NbExp=3; IntAct=EBI-12808020, EBI-12200293;
CC Q9BZJ8; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-12808020, EBI-348587;
CC Q9BZJ8; A2RU14: TMEM218; NbExp=3; IntAct=EBI-12808020, EBI-10173151;
CC Q9BZJ8; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-12808020, EBI-2852148;
CC Q9BZJ8; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-12808020, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28827538,
CC ECO:0000269|PubMed:29226084}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:28827538}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Colocalizes with ARRB2/beta-
CC arrestin-2 in the endosome (PubMed:28827538).
CC {ECO:0000269|PubMed:28827538}.
CC -!- TISSUE SPECIFICITY: Expressed in brain; detected in frontal and
CC temporal lobes, occipital pole, amygdala and hippocampus
CC (PubMed:11690637, PubMed:29226084). Also expressed in testis
CC (PubMed:11690637, PubMed:29226084) and T cells, B cells, and monocyte
CC (PubMed:29226084). Low expression in many other tissues
CC (PubMed:11690637, PubMed:29226084). Widely expressed in the hippocampus
CC (at protein level). {ECO:0000269|PubMed:11690637,
CC ECO:0000269|PubMed:29226084}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK12637.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF317652; AAK12637.1; ALT_FRAME; mRNA.
DR EMBL; AF258342; AAK97826.1; -; mRNA.
DR EMBL; AB083585; BAB89298.1; -; Genomic_DNA.
DR EMBL; AK290027; BAF82716.1; -; mRNA.
DR EMBL; AL355310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56392.1; -; Genomic_DNA.
DR EMBL; BC067464; AAH67464.1; -; mRNA.
DR CCDS; CCDS801.1; -.
DR RefSeq; NP_114142.3; NM_031936.4.
DR RefSeq; XP_016857927.1; XM_017002438.1.
DR AlphaFoldDB; Q9BZJ8; -.
DR SMR; Q9BZJ8; -.
DR BioGRID; 123786; 20.
DR IntAct; Q9BZJ8; 20.
DR STRING; 9606.ENSP00000432456; -.
DR ChEMBL; CHEMBL4523918; -.
DR GlyGen; Q9BZJ8; 1 site.
DR iPTMnet; Q9BZJ8; -.
DR PhosphoSitePlus; Q9BZJ8; -.
DR BioMuta; GPR61; -.
DR DMDM; 76789653; -.
DR PaxDb; Q9BZJ8; -.
DR PeptideAtlas; Q9BZJ8; -.
DR PRIDE; Q9BZJ8; -.
DR ProteomicsDB; 79862; -.
DR Antibodypedia; 1935; 182 antibodies from 26 providers.
DR DNASU; 83873; -.
DR Ensembl; ENST00000404129.6; ENSP00000385422.2; ENSG00000156097.13.
DR Ensembl; ENST00000469383.2; ENSP00000433661.1; ENSG00000156097.13.
DR Ensembl; ENST00000527748.5; ENSP00000432456.1; ENSG00000156097.13.
DR Ensembl; ENST00000616874.2; ENSP00000484035.1; ENSG00000156097.13.
DR Ensembl; ENST00000618721.5; ENSP00000484797.1; ENSG00000156097.13.
DR GeneID; 83873; -.
DR KEGG; hsa:83873; -.
DR MANE-Select; ENST00000527748.5; ENSP00000432456.1; NM_001393907.1; NP_001380836.1.
DR UCSC; uc001dxy.2; human.
DR CTD; 83873; -.
DR DisGeNET; 83873; -.
DR GeneCards; GPR61; -.
DR HGNC; HGNC:13300; GPR61.
DR HPA; ENSG00000156097; Group enriched (brain, pituitary gland, retina).
DR MIM; 606916; gene.
DR neXtProt; NX_Q9BZJ8; -.
DR OpenTargets; ENSG00000156097; -.
DR PharmGKB; PA28905; -.
DR VEuPathDB; HostDB:ENSG00000156097; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182998; -.
DR HOGENOM; CLU_009579_3_1_1; -.
DR InParanoid; Q9BZJ8; -.
DR OMA; GGQFLFC; -.
DR OrthoDB; 901432at2759; -.
DR PhylomeDB; Q9BZJ8; -.
DR TreeFam; TF332667; -.
DR PathwayCommons; Q9BZJ8; -.
DR SignaLink; Q9BZJ8; -.
DR BioGRID-ORCS; 83873; 174 hits in 1069 CRISPR screens.
DR GeneWiki; GPR61; -.
DR GenomeRNAi; 83873; -.
DR Pharos; Q9BZJ8; Tbio.
DR PRO; PR:Q9BZJ8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BZJ8; protein.
DR Bgee; ENSG00000156097; Expressed in prefrontal cortex and 90 other tissues.
DR ExpressionAtlas; Q9BZJ8; baseline and differential.
DR Genevisible; Q9BZJ8; HS.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:1990763; F:arrestin family protein binding; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 membrane; Endosome; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..451
FT /note="G-protein coupled receptor 61"
FT /id="PRO_0000069578"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..112
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..310
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29226084"
FT MUTAGEN 12
FT /note="N->S: Does not affect subcellular location."
FT /evidence="ECO:0000269|PubMed:29226084"
FT CONFLICT 91
FT /note="L -> P (in Ref. 2; AAK97826)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="S -> P (in Ref. 1; AAK12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="V -> M (in Ref. 2; AAK97826)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="G -> H (in Ref. 1; AAK12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="V -> L (in Ref. 1; AAK12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="QH -> PD (in Ref. 1; AAK12637)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="E -> K (in Ref. 7; AAH67464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 49292 MW; 1F477F112E1CEA1A CRC64;
MESSPIPQSS GNSSTLGRVP QTPGPSTASG VPEVGLRDVA SESVALFFML LLDLTAVAGN
AAVMAVIAKT PALRKFVFVF HLCLVDLLAA LTLMPLAMLS SSALFDHALF GEVACRLYLF
LSVCFVSLAI LSVSAINVER YYYVVHPMRY EVRMTLGLVA SVLVGVWVKA LAMASVPVLG
RVSWEEGAPS VPPGCSLQWS HSAYCQLFVV VFAVLYFLLP LLLILVVYCS MFRVARVAAM
QHGPLPTWME TPRQRSESLS SRSTMVTSSG APQTTPHRTF GGGKAAVVLL AVGGQFLLCW
LPYFSFHLYV ALSAQPISTG QVESVVTWIG YFCFTSNPFF YGCLNRQIRG ELSKQFVCFF
KPAPEEELRL PSREGSIEEN FLQFLQGTGC PSESWVSRPL PSPKQEPPAV DFRIPGQIAE
ETSEFLEQQL TSDIIMSDSY LRPAASPRLE S
