ID   AGRL2_MOUSE             Reviewed;        1487 AA.
AC   Q8JZZ7; E9Q6C7; Q8BM90;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 3.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Adhesion G protein-coupled receptor L2;
DE   AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE            Short=CIRL-2;
DE   AltName: Full=Latrophilin-2;
DE   Flags: Precursor;
GN   Name=Adgrl2; Synonyms=Kiaa0786, Lphn2;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-1487 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 740-747, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1015-1487 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1256-1487.
RC   TISSUE=Retina;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1402 AND SER-1458, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-735.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-735.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437 AND SER-1458, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and 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).
RN   [10]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX   PubMed=24273166; DOI=10.1074/jbc.m113.504779;
RA   Boucard A.A., Maxeiner S., Suedhof T.C.;
RT   "Latrophilins function as heterophilic cell-adhesion molecules by binding
RT   to teneurins: regulation by alternative splicing.";
RL   J. Biol. Chem. 289:387-402(2014).
CC   -!- FUNCTION: Calcium-independent receptor of low affinity for alpha-
CC       latrotoxin, an excitatory neurotoxin present in black widow spider
CC       venom which triggers massive exocytosis from neurons and neuroendocrine
CC       cells. Receptor probably implicated in the regulation of exocytosis.
CC       {ECO:0000250|UniProtKB:O88923, ECO:0000269|PubMed:24273166}.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region non-covalently linked to a seven-transmembrane moiety.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8JZZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8JZZ7-2; Sequence=VSP_010110, VSP_010111;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:24273166}.
CC   -!- DEVELOPMENTAL STAGE: Decrease in mRNA levels during postnatal
CC       development. {ECO:0000269|PubMed:19349973}.
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC       and a seven-transmembrane subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH34660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC113315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK129215; BAC98025.1; -; mRNA.
DR   EMBL; AK034430; BAC28707.1; -; mRNA.
DR   EMBL; BC034660; AAH34660.1; ALT_INIT; mRNA.
DR   CCDS; CCDS80059.1; -. [Q8JZZ7-1]
DR   PDB; 6SKE; X-ray; 3.62 A; B/D=30-137.
DR   PDBsum; 6SKE; -.
DR   AlphaFoldDB; Q8JZZ7; -.
DR   SMR; Q8JZZ7; -.
DR   IntAct; Q8JZZ7; 2.
DR   MINT; Q8JZZ7; -.
DR   STRING; 10090.ENSMUSP00000143626; -.
DR   MEROPS; P02.009; -.
DR   GlyConnect; 2418; 4 N-Linked glycans (1 site). [Q8JZZ7-2]
DR   GlyCosmos; Q8JZZ7; 4 sites, 4 glycans.
DR   GlyGen; Q8JZZ7; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8JZZ7; -.
DR   PhosphoSitePlus; Q8JZZ7; -.
DR   SwissPalm; Q8JZZ7; -.
DR   jPOST; Q8JZZ7; -.
DR   MaxQB; Q8JZZ7; -.
DR   PaxDb; 10090-ENSMUSP00000101734; -.
DR   PeptideAtlas; Q8JZZ7; -.
DR   ProteomicsDB; 285774; -. [Q8JZZ7-1]
DR   ProteomicsDB; 285775; -. [Q8JZZ7-2]
DR   Pumba; Q8JZZ7; -.
DR   Antibodypedia; 2953; 168 antibodies from 29 providers.
DR   Ensembl; ENSMUST00000106128.7; ENSMUSP00000101734.3; ENSMUSG00000028184.13. [Q8JZZ7-1]
DR   UCSC; uc008rsa.1; mouse. [Q8JZZ7-1]
DR   UCSC; uc008rsb.1; mouse.
DR   AGR; MGI:2139714; -.
DR   MGI; MGI:2139714; Adgrl2.
DR   VEuPathDB; HostDB:ENSMUSG00000028184; -.
DR   eggNOG; KOG3545; Eukaryota.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; KOG4729; Eukaryota.
DR   GeneTree; ENSGT00940000156348; -.
DR   InParanoid; Q8JZZ7; -.
DR   PhylomeDB; Q8JZZ7; -.
DR   TreeFam; TF351999; -.
DR   ChiTaRS; Adgrl2; mouse.
DR   PRO; PR:Q8JZZ7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8JZZ7; Protein.
DR   Bgee; ENSMUSG00000028184; Expressed in manus and 225 other cell types or tissues.
DR   ExpressionAtlas; Q8JZZ7; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
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   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0050808; P:synapse organization; IDA:SynGO.
DR   CDD; cd22845; Gal_Rha_Lectin_LPHN2; 1.
DR   Gene3D; 1.25.40.610; -; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR003924; GPCR_2_latrophilin.
DR   InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR12011:SF61; ADHESION G PROTEIN-COUPLED RECEPTOR L2; 1.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF02354; Latrophilin; 1.
DR   Pfam; PF02191; OLF; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01444; LATROPHILIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00284; OLF; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51132; OLF; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1487
FT                   /note="Adhesion G protein-coupled receptor L2"
FT                   /id="PRO_0000070343"
FT   TOPO_DOM        26..855
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        856..876
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        877..884
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        885..905
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        906..911
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        912..932
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        933..955
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        956..976
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        977..994
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        995..1015
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1016..1064
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1065..1085
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1086..1090
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1091..1111
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          41..130
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          139..398
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DOMAIN          789..840
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          423..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1386..1430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1386..1409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            828..829
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         1437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        735
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   VAR_SEQ         1062
FT                   /note="K -> NNYRVCDGYYNTDLPG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010110"
FT   VAR_SEQ         1194
FT                   /note="G -> GMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPAFNSPATYR
FT                   ETR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010111"
SQ   SEQUENCE   1487 AA;  166577 MW;  A56F7A5409E801F8 CRC64;
     MVSSGCRMRS LWFIIIISFS PSTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
     SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
     KYLEVQYECV PYSKMLVFVC PGTLKAIVDS PCIYEAEQKS GAWCKDPLQA ADKIYFMPWT
     PYRTDTLIEY ASLEDFQNSR QTTTYKLPNR VDGTGFVVYD GAVFFNKERT RNIVKFDLRT
     RIKSGEAIIN YANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEQNNGMI VISQLNPYTL
     RFEATWETAY DKRAASNAFM ICGVLYVVRS VYQDNESEAG KNTIDYIYNT RLSRGEYVDV
     PFPNQYQYIA AVDYNPRDNQ LYVWNNNFIL RYSLEFGPPD PAQVPTTAVT ITSSAELFKT
     TISTTSSASQ RGPVSSTAAG PQDGSRGTKP PPAVSTTKIP PVTNIFPLPE RFCEALDWKG
     IKWPQTQRGM MVERPCPKGT RGTASYLCMA STGTWNPKGP DLSNCTSHWV NQLAQKIRSG
     ENAASLANEL AKHTKGHVFA GDVSSSVRLM EQLVDILDAQ LQELKPSEKD SAGRSYNKLQ
     KREKTCRAYL KAIVDTVDNL LRAEALESWK HMNSSEQAHT ATMLLDTLEE GAFVLADNLL
     EPTRVSMPTE NIVLEVAVLS TEGQVQDFKF PLGLKGLGSS IQLSANTVKQ NSRNGLAKLV
     FIIYRSLGQF LSTENATIKL GADLMGRNST IAVNSPVISV SINKESSRVY LTDPVLFTLP
     HIDPDNYFNA NCSFWNYSER TMMGYWSTQG CKLVDTNKTR TTCACSHLTN FAILMAHREI
     AYKDGVHHLL LTVITWVGIV VSLVCLAICI FTFCFFRGLQ SDRNTIHKNL CINLFIAEFI
     FLIGIDKTKY TIACPVFAGL LHFFFLAAFS WMCLEGVQLY LMLVEVFESE YSRKKYYYVA
     GYLFPATVVG VSAAIDYKSY GTVQACWLHV DNYFIWSFIG PVTFIILLNI IFLVITLCKM
     VKHSNTLKPD SSRLENINNY RVCDGYYNTD LPGYEDNKPF IKSWVLGAFA LLCLLGLTWS
     FGLLFVNEET VVMAYLFTAF NAFQGLFIFI FHCALQKKVR KEYGKCFRHW YCCGGLPTES
     PHSSVKASTT RTSARYSSGT QSRIRRMWND TVRKQSESSF ISGDINSTST LNQGMTGNYL
     LTNPLLRPHG TNNPYNTLLA ETVVCNAPSA PAFNSPGHSL NNARDTSAMD TLPLNGNFNN
     SYSLRKADYH DGVQVVDCGL SLNDTAFEKM IISELVHNNL RGGNKTHNLE LKLPVKPVIG
     GSSSEDDAIV ADASSLMHGD NPGLEFRHKE LEAPLIPQRT HSLLYQPQKK VKPEATDSYV
     SQLTAEADDH LQSPNRDSLY TSMPNLRDSP YPESSPDMAE DLSPSRRSEN EDIYYKSMPN
     LGAGRHLHMC YQISRGNSDG YIIPINKEGC IPEGDVREGQ MQLVTSL
//