AGRG2_MOUSE
ID AGRG2_MOUSE Reviewed; 1009 AA.
AC Q8CJ12; A2AHP8; A2AHP9; A2AHQ0; A2AHQ3; Q8BL10; Q8CJ08; Q8CJ09; Q8CJ10;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Adhesion G-protein coupled receptor G2;
DE AltName: Full=G-protein coupled receptor 64;
DE AltName: Full=Mouse epididymis-specific protein 6;
DE Short=Me6;
DE Flags: Precursor;
GN Name=Adgrg2 {ECO:0000312|MGI:MGI:2446854}; Synonyms=Gpr64, Me6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), TISSUE SPECIFICITY,
RP SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=NMRI; TISSUE=Epididymis;
RX PubMed=12420295; DOI=10.1002/mrd.10220;
RA Obermann H., Samalecos A., Osterhoff C., Schroeder B., Heller R.,
RA Kirchhoff C.;
RT "HE6, a two-subunit heptahelical receptor associated with apical membranes
RT of efferent and epididymal duct epithelia.";
RL Mol. Reprod. Dev. 64:13-26(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15367682; DOI=10.1128/mcb.24.19.8642-8648.2004;
RA Davies B., Baumann C., Kirchhoff C., Ivell R., Nubbemeyer R.,
RA Habenicht U.F., Theuring F., Gottwald U.;
RT "Targeted deletion of the epididymal receptor HE6 results in fluid
RT dysregulation and male infertility.";
RL Mol. Cell. Biol. 24:8642-8648(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=18469038; DOI=10.1530/rep-08-0078;
RA Kirchhoff C., Osterhoff C., Samalecos A.;
RT "HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin
RT scaffold in male excurrent duct epithelia.";
RL Reproduction 136:235-245(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1002, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Orphan receptor. Could be involved in a signal transduction
CC pathway controlling epididymal function and male fertility. May
CC regulate fluid exchange within epididymis.
CC {ECO:0000269|PubMed:15367682}.
CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Long;
CC IsoId=Q8CJ12-1; Sequence=Displayed;
CC Name=2; Synonyms=d2;
CC IsoId=Q8CJ12-2; Sequence=VSP_009808;
CC Name=3; Synonyms=d1;
CC IsoId=Q8CJ12-3; Sequence=VSP_009809;
CC Name=4; Synonyms=d3;
CC IsoId=Q8CJ12-4; Sequence=VSP_009807;
CC Name=5;
CC IsoId=Q8CJ12-5; Sequence=VSP_009806;
CC -!- TISSUE SPECIFICITY: Epididymis-specific expression (at protein level).
CC Associated with apical membranes of efferent ductule and proximal
CC epididymal duct epithelia. Mainly expressed in the nonciliated
CC principal cells of the proximal excurrent ducts.
CC {ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:18469038}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000305}.
CC -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}.
CC -!- DISRUPTION PHENOTYPE: Mutant male are infertile. Targeted disruption
CC leads to sperm stasis and duct obstruction, resulting from
CC dysregulation of fluid reabsorption. {ECO:0000269|PubMed:15367682}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AF538952; AAN33054.1; -; mRNA.
DR EMBL; AF538955; AAN33057.1; -; mRNA.
DR EMBL; AF538956; AAN33058.1; -; mRNA.
DR EMBL; AF538957; AAN33059.1; -; mRNA.
DR EMBL; AK046871; BAC32902.1; -; mRNA.
DR EMBL; AL731801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41196.1; -. [Q8CJ12-1]
DR CCDS; CCDS41197.1; -. [Q8CJ12-3]
DR CCDS; CCDS41199.1; -. [Q8CJ12-5]
DR CCDS; CCDS72459.1; -. [Q8CJ12-2]
DR CCDS; CCDS81192.1; -. [Q8CJ12-4]
DR RefSeq; NP_001073317.1; NM_001079848.2. [Q8CJ12-5]
DR RefSeq; NP_001073326.1; NM_001079857.2. [Q8CJ12-3]
DR RefSeq; NP_001277374.1; NM_001290445.1. [Q8CJ12-4]
DR RefSeq; NP_001277375.1; NM_001290446.1. [Q8CJ12-2]
DR RefSeq; NP_848827.1; NM_178712.4. [Q8CJ12-1]
DR AlphaFoldDB; Q8CJ12; -.
DR SMR; Q8CJ12; -.
DR STRING; 10090.ENSMUSP00000108019; -.
DR MEROPS; P02.007; -.
DR GlyGen; Q8CJ12; 20 sites.
DR iPTMnet; Q8CJ12; -.
DR PhosphoSitePlus; Q8CJ12; -.
DR MaxQB; Q8CJ12; -.
DR PaxDb; Q8CJ12; -.
DR PRIDE; Q8CJ12; -.
DR ProteomicsDB; 296133; -. [Q8CJ12-1]
DR ProteomicsDB; 296134; -. [Q8CJ12-2]
DR ProteomicsDB; 296135; -. [Q8CJ12-3]
DR ProteomicsDB; 296136; -. [Q8CJ12-4]
DR ProteomicsDB; 296137; -. [Q8CJ12-5]
DR Antibodypedia; 473; 132 antibodies from 25 providers.
DR DNASU; 237175; -.
DR Ensembl; ENSMUST00000112400; ENSMUSP00000108019; ENSMUSG00000031298. [Q8CJ12-1]
DR Ensembl; ENSMUST00000112402; ENSMUSP00000108021; ENSMUSG00000031298. [Q8CJ12-3]
DR Ensembl; ENSMUST00000112404; ENSMUSP00000108023; ENSMUSG00000031298. [Q8CJ12-5]
DR Ensembl; ENSMUST00000112405; ENSMUSP00000108024; ENSMUSG00000031298. [Q8CJ12-4]
DR Ensembl; ENSMUST00000112408; ENSMUSP00000108027; ENSMUSG00000031298. [Q8CJ12-2]
DR GeneID; 237175; -.
DR KEGG; mmu:237175; -.
DR UCSC; uc009utd.2; mouse. [Q8CJ12-1]
DR UCSC; uc009ute.2; mouse. [Q8CJ12-3]
DR UCSC; uc009utg.2; mouse. [Q8CJ12-5]
DR UCSC; uc009uth.2; mouse. [Q8CJ12-2]
DR UCSC; uc009uti.2; mouse. [Q8CJ12-4]
DR CTD; 10149; -.
DR MGI; MGI:2446854; Adgrg2.
DR VEuPathDB; HostDB:ENSMUSG00000031298; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000156341; -.
DR HOGENOM; CLU_002753_3_3_1; -.
DR InParanoid; Q8CJ12; -.
DR OMA; NKTMNVC; -.
DR OrthoDB; 148879at2759; -.
DR PhylomeDB; Q8CJ12; -.
DR TreeFam; TF321769; -.
DR BioGRID-ORCS; 237175; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Adgrg2; mouse.
DR PRO; PR:Q8CJ12; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8CJ12; protein.
DR Bgee; ENSMUSG00000031298; Expressed in efferent duct and 119 other tissues.
DR ExpressionAtlas; Q8CJ12; baseline and differential.
DR Genevisible; Q8CJ12; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1009
FT /note="Adhesion G-protein coupled receptor G2"
FT /id="PRO_0000012887"
FT TOPO_DOM 38..619
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 620..640
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 660..680
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..683
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 684..704
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 730..750
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 751..781
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 782..802
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 803..826
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 827..847
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..849
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 850..870
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..1009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 559..610
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 279..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 40..66
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12420295"
FT /id="VSP_009806"
FT VAR_SEQ 51..66
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12420295"
FT /id="VSP_009807"
FT VAR_SEQ 64..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12420295"
FT /id="VSP_009808"
FT VAR_SEQ 80..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009809"
FT CONFLICT 781
FT /note="T -> K (in Ref. 2; BAC32902)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 110200 MW; A53C67C5527A5B6C CRC64;
MLFSGGQYSP VGRPEEVLLI YKIFLVIICF HVILVTSLKE NGNSSLLSPS AESSLVSLIP
YSNGTPDAAS EVLSTLNKTE KSKITIVKTF NASGVKSQRN ICNLSSLCND SVFFRGEIVF
QHDEDHNVTQ NQDTANGTFA GVLSLSELKR SELNKTLQTL SETYFIVCAT AEAQSTVNCT
FTVKLNETMN VCAMMVTFQT VQIRPMEQCC CSPRTPCPSS PEELEKLQCE LQDPIVCLAD
QPHGPPLSSS SKPVVPQATI ISHVASDFSL AEPLDHALMT PSTPSLTQES NLPSPQPTIP
LASSPATDLP VQSVVVSSLP QTDLSHTLSP VQSSIPSPTT PAPSVPTELV TISTPPGETV
VNTSTVSDLE AQVSQMEKAL SLGSLEPNLA GEMVNRVSKL LHSPPALLAP LAQRLLKVVD
AIGLQLNFSS TTISLTSPSL ALAVIRVNAS NFNTTTFAAQ DPTNLQVSLE TPPPENSIGA
ITLPSSLMNN LPANDVELAS RIQFNFFETP ALFQDPSLEN LTLISYVISS SVTNMTIKNL
TRNVTVALKH INPSPDDLTV KCVFWDLGRN GGKGGWSSDG CSVKDKRMNE TICTCSHLTS
FGILLDLSRT SLPPSQMMAL TFITYIGCGL SSIFLSVTLV TYIAFEKIRR DYPSKILIQL
CAALLLLNLI FLLDSWIALY NTRGFCIAVA VFLHYFLLVS FTWMGLEAFH MYLALVKVFN
TYIRKYILKF CIVGWGIPAV VVSIVLTISP DNYGIGSYGK FPNGTPDDFC WINSNVVFYI
TVVGYFCVIF LLNVSMFIVV LVQLCRIKKK KQLGAQRKTS IQDLRSIAGL TFLLGITWGF
AFFAWGPVNV TFMYLFAIFN TLQGFFIFIF YCAAKENVRK QWRRYLCCGK LRLAENSDWS
KTATNGLKKQ TVNQGVSSSS NSLQSSCNST NSTTLLVNSD CSVHASGNGN ASTERNGVSF
SVQNGDVCLH DLTGKQHMFS DKEDSCNGKS RIALRRTSKR GSLHFIEQM
