GP161_HUMAN
ID GP161_HUMAN Reviewed; 529 AA.
AC Q8N6U8; B3KV34; B7Z5D7; B7Z5E8; B7Z5Z6; F5GXD6; F5H6J7; O75963; Q5TGK0;
AC Q5TGK1; Q5TGK2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=G-protein coupled receptor 161;
DE AltName: Full=G-protein coupled receptor RE2;
GN Name=GPR161;
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).
RC TISSUE=Brain;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "Isolation of cDNA coding for G-protein coupled receptor RE2.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=9932290;
RA Raming K., Konzelmann S., Breer H.;
RT "Identification of a novel G-protein coupled receptor expressed in distinct
RT brain regions and a defined olfactory zone.";
RL Recept. Channels 6:141-151(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4; 5 AND 6).
RC TISSUE=Brain, and Teratocarcinoma;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
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).
CC -!- FUNCTION: Key negative regulator of Shh signaling, which promotes the
CC processing of GLI3 into GLI3R during neural tube development. Recruited
CC by TULP3 and the IFT-A complex to primary cilia and acts as a regulator
CC of the PKA-dependent basal repression machinery in Shh signaling by
CC increasing cAMP levels, leading to promote the PKA-dependent processing
CC of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH,
CC it is removed from primary cilia and is internalized into recycling
CC endosomes, preventing its activity and allowing activation of the Shh
CC signaling. Its ligand is unknown (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N6U8; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-6255622, EBI-12256978;
CC Q8N6U8; P21964: COMT; NbExp=3; IntAct=EBI-6255622, EBI-372265;
CC Q8N6U8; P52803: EFNA5; NbExp=3; IntAct=EBI-6255622, EBI-1753674;
CC Q8N6U8; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-6255622, EBI-8644112;
CC Q8N6U8; O75841: UPK1B; NbExp=3; IntAct=EBI-6255622, EBI-12237619;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to
CC primary cilium in a TULP3 and IFT-A complex-dependent manner. In
CC presence of SHH, it is removed from primary cilia and is internalized
CC into recycling endosomes and is apparently not degraded (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8N6U8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6U8-2; Sequence=VSP_010560, VSP_010561;
CC Name=3;
CC IsoId=Q8N6U8-3; Sequence=VSP_035561;
CC Name=4;
CC IsoId=Q8N6U8-4; Sequence=VSP_044778, VSP_044779;
CC Name=5;
CC IsoId=Q8N6U8-5; Sequence=VSP_045329;
CC Name=6;
CC IsoId=Q8N6U8-6; Sequence=VSP_046299;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY275468; AAP32300.1; -; mRNA.
DR EMBL; AF091890; AAC61598.1; -; mRNA.
DR EMBL; AK056040; BAG51611.1; -; mRNA.
DR EMBL; AK122656; BAG53646.1; -; mRNA.
DR EMBL; AK298797; BAH12873.1; -; mRNA.
DR EMBL; AK298850; BAH12884.1; -; mRNA.
DR EMBL; AK299634; BAH13082.1; -; mRNA.
DR EMBL; AL033532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028163; AAH28163.1; -; mRNA.
DR CCDS; CCDS1268.1; -. [Q8N6U8-1]
DR CCDS; CCDS58042.1; -. [Q8N6U8-3]
DR CCDS; CCDS58043.1; -. [Q8N6U8-6]
DR CCDS; CCDS58044.1; -. [Q8N6U8-4]
DR CCDS; CCDS58045.1; -. [Q8N6U8-5]
DR RefSeq; NP_001254538.1; NM_001267609.1. [Q8N6U8-6]
DR RefSeq; NP_001254539.1; NM_001267610.1. [Q8N6U8-1]
DR RefSeq; NP_001254541.1; NM_001267612.1. [Q8N6U8-3]
DR RefSeq; NP_001254542.1; NM_001267613.1. [Q8N6U8-4]
DR RefSeq; NP_001254543.1; NM_001267614.1. [Q8N6U8-5]
DR RefSeq; NP_722561.1; NM_153832.2. [Q8N6U8-1]
DR RefSeq; XP_005245112.1; XM_005245055.2. [Q8N6U8-6]
DR RefSeq; XP_005245113.1; XM_005245056.2.
DR RefSeq; XP_005245114.1; XM_005245057.4.
DR RefSeq; XP_011507677.1; XM_011509375.2.
DR RefSeq; XP_011507678.1; XM_011509376.2. [Q8N6U8-1]
DR RefSeq; XP_011507679.1; XM_011509377.1.
DR RefSeq; XP_011507680.1; XM_011509378.1.
DR RefSeq; XP_016856348.1; XM_017000859.1.
DR RefSeq; XP_016856349.1; XM_017000860.1.
DR RefSeq; XP_016856350.1; XM_017000861.1.
DR RefSeq; XP_016856351.1; XM_017000862.1.
DR AlphaFoldDB; Q8N6U8; -.
DR SMR; Q8N6U8; -.
DR BioGRID; 117000; 29.
DR IntAct; Q8N6U8; 23.
DR MINT; Q8N6U8; -.
DR STRING; 9606.ENSP00000441039; -.
DR ChEMBL; CHEMBL4523894; -.
DR TCDB; 9.A.14.1.11; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q8N6U8; 2 sites.
DR iPTMnet; Q8N6U8; -.
DR PhosphoSitePlus; Q8N6U8; -.
DR BioMuta; GPR161; -.
DR DMDM; 48428085; -.
DR EPD; Q8N6U8; -.
DR jPOST; Q8N6U8; -.
DR MassIVE; Q8N6U8; -.
DR PaxDb; Q8N6U8; -.
DR PeptideAtlas; Q8N6U8; -.
DR PRIDE; Q8N6U8; -.
DR ProteomicsDB; 24390; -.
DR ProteomicsDB; 27210; -.
DR ProteomicsDB; 6685; -.
DR ProteomicsDB; 72236; -. [Q8N6U8-1]
DR ProteomicsDB; 72238; -. [Q8N6U8-3]
DR TopDownProteomics; Q8N6U8-1; -. [Q8N6U8-1]
DR Antibodypedia; 2941; 280 antibodies from 31 providers.
DR DNASU; 23432; -.
DR Ensembl; ENST00000367835.1; ENSP00000356809.1; ENSG00000143147.15. [Q8N6U8-1]
DR Ensembl; ENST00000367836.5; ENSP00000356810.1; ENSG00000143147.15. [Q8N6U8-3]
DR Ensembl; ENST00000367838.5; ENSP00000356812.1; ENSG00000143147.15. [Q8N6U8-1]
DR Ensembl; ENST00000537209.5; ENSP00000441039.1; ENSG00000143147.15. [Q8N6U8-6]
DR Ensembl; ENST00000539777.5; ENSP00000437576.1; ENSG00000143147.15. [Q8N6U8-4]
DR Ensembl; ENST00000546300.5; ENSP00000444348.1; ENSG00000143147.15. [Q8N6U8-5]
DR Ensembl; ENST00000682931.1; ENSP00000506967.1; ENSG00000143147.15. [Q8N6U8-1]
DR GeneID; 23432; -.
DR KEGG; hsa:23432; -.
DR MANE-Select; ENST00000682931.1; ENSP00000506967.1; NM_001375883.1; NP_001362812.1.
DR UCSC; uc001gfb.5; human. [Q8N6U8-1]
DR CTD; 23432; -.
DR DisGeNET; 23432; -.
DR GeneCards; GPR161; -.
DR HGNC; HGNC:23694; GPR161.
DR HPA; ENSG00000143147; Tissue enhanced (endometrium, smooth muscle).
DR MalaCards; GPR161; -.
DR MIM; 612250; gene.
DR neXtProt; NX_Q8N6U8; -.
DR OpenTargets; ENSG00000143147; -.
DR Orphanet; 95496; Pituitary stalk interruption syndrome.
DR PharmGKB; PA134931474; -.
DR VEuPathDB; HostDB:ENSG00000143147; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157829; -.
DR HOGENOM; CLU_038027_0_0_1; -.
DR InParanoid; Q8N6U8; -.
DR OrthoDB; 1262707at2759; -.
DR PhylomeDB; Q8N6U8; -.
DR TreeFam; TF331895; -.
DR PathwayCommons; Q8N6U8; -.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR SignaLink; Q8N6U8; -.
DR SIGNOR; Q8N6U8; -.
DR BioGRID-ORCS; 23432; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; GPR161; human.
DR GeneWiki; GPR161; -.
DR GenomeRNAi; 23432; -.
DR Pharos; Q8N6U8; Tbio.
DR PRO; PR:Q8N6U8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N6U8; protein.
DR Bgee; ENSG00000143147; Expressed in cortical plate and 188 other tissues.
DR ExpressionAtlas; Q8N6U8; baseline and differential.
DR Genevisible; Q8N6U8; HS.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0097386; C:glial cell projection; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISS: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 Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Developmental protein; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..529
FT /note="G-protein coupled receptor 161"
FT /id="PRO_0000069646"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035561"
FT VAR_SEQ 1..125
FT /note="MSLNSSLSCRKELSNLTEEEGGEGGVIITQFIAIIVITIFVCLGNLVIVVTL
FT YKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLIS
FT SASMLTLGVIAIDR -> MLVPVGWMNES (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045329"
FT VAR_SEQ 1..47
FT /note="MSLNSSLSCRKELSNLTEEEGGEGGVIITQFIAIIVITIFVCLGNLV -> M
FT GGRRCVPGTLPMRAAPPGAKRLHVPLRAKGVGRSGHAPRLESVRTS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044778"
FT VAR_SEQ 1
FT /note="M -> MSARGVVQHALPTPRRGALTM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046299"
FT VAR_SEQ 48..125
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044779"
FT VAR_SEQ 403..407
FT /note="TDMML -> NLRAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9932290"
FT /id="VSP_010560"
FT VAR_SEQ 408..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9932290"
FT /id="VSP_010561"
FT CONFLICT 193
FT /note="Q -> R (in Ref. 3; BAH12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="W -> R (in Ref. 3; BAH13082)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="Y -> N (in Ref. 3; BAH12873)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="C -> S (in Ref. 3; BAH13082)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> V (in Ref. 3; BAH12873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 58559 MW; FC7D1AC0894DC3F3 CRC64;
MSLNSSLSCR KELSNLTEEE GGEGGVIITQ FIAIIVITIF VCLGNLVIVV TLYKKSYLLT
LSNKFVFSLT LSNFLLSVLV LPFVVTSSIR REWIFGVVWC NFSALLYLLI SSASMLTLGV
IAIDRYYAVL YPMVYPMKIT GNRAVMALVY IWLHSLIGCL PPLFGWSSVE FDEFKWMCVA
AWHREPGYTA FWQIWCALFP FLVMLVCYGF IFRVARVKAR KVHCGTVVIV EEDAQRTGRK
NSSTSTSSSG SRRNAFQGVV YSANQCKALI TILVVLGAFM VTWGPYMVVI ASEALWGKSS
VSPSLETWAT WLSFASAVCH PLIYGLWNKT VRKELLGMCF GDRYYREPFV QRQRTSRLFS
ISNRITDLGL SPHLTALMAG GQPLGHSSST GDTGFSCSQD SGTDMMLLED YTSDDNPPSH
CTCPPKRRSS VTFEDEVEQI KEAAKNSILH VKAEVHKSLD SYAASLAKAI EAEAKINLFG
EEALPGVLVT ARTVPGGGFG GRRGSRTLVS QRLQLQSIEE GDVLAAEQR
