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
//
