ID AGRL3_RAT Reviewed; 1550 AA.
AC Q9Z173; O88924; O88925; O88926; O88927; O88928; O88929; Q4LDM4; Q4LDM5;
AC Q4LDM6; Q4LDM7; Q4LDM8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000312|RGD:620836};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 3 {ECO:0000303|PubMed:10026162};
DE Short=CIRL-3 {ECO:0000303|PubMed:10026162};
DE AltName: Full=Latrophilin-3 {ECO:0000312|RGD:620836};
DE Flags: Precursor;
GN Name=Adgrl3 {ECO:0000312|RGD:620836};
GN Synonyms=Cirl3 {ECO:0000303|PubMed:10026162},
GN Cl3 {ECO:0000303|PubMed:9830014}, Lphn3 {ECO:0000312|RGD:620836};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7).
RX PubMed=9830014; DOI=10.1074/jbc.273.49.32715;
RA Sugita S., Ichtchenko K., Khvotchev M., Suedhof T.C.;
RT "Alpha-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual
RT family of ubiquitous G-protein-linked receptors. G-protein coupling not
RT required for triggering exocytosis.";
RL J. Biol. Chem. 273:32715-32724(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10026162; DOI=10.1074/jbc.274.9.5491;
RA Ichtchenko K., Bittner M.A., Krasnoperov V., Little A.R., Chepurny O.,
RA Holz R.W., Petrenko A.G.;
RT "A novel ubiquitously expressed alpha-latrotoxin receptor is a member of
RT the CIRL family of G-protein-coupled receptors.";
RL J. Biol. Chem. 274:5491-5498(1999).
RN [3]
RP INTERACTION WITH FLRT3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
CC -!- FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via
CC its interactions with FLRT2 and FLRT3 that are expressed at the surface
CC of adjacent cells. Plays a role in the development of glutamatergic
CC synapses in the cortex. Important in determining the connectivity rates
CC between the principal neurons in the cortex.
CC {ECO:0000250|UniProtKB:Q80TS3}.
CC -!- SUBUNIT: Interacts (via olfactomedin-like domain) with FLRT3 (via
CC extracellular domain); the interaction is direct (PubMed:22405201).
CC Identified in a complex with FLRT3 and UNC5B; does not interact with
CC UNC5B by itself. Identified in a complex with FLRT3 and UNC5D; does not
CC interact with UNC5D by itself (By similarity). Interacts (via
CC olfactomedin-like domain) with FLRT1 (via extracellular domain).
CC Interacts (via olfactomedin-like domain) with FLRT2 (via extracellular
CC domain). Interacts (via extracellular domain) with TENM1. Interacts
CC (via extracellular domain) with TENM3 (By similarity).
CC {ECO:0000250|UniProtKB:Q80TS3, ECO:0000250|UniProtKB:Q9HAR2,
CC ECO:0000269|PubMed:22405201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80TS3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80TS3}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction
CC {ECO:0000250|UniProtKB:Q80TS3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q9Z173-1; Sequence=Displayed;
CC Name=2; Synonyms=CL3AA;
CC IsoId=Q9Z173-2; Sequence=VSP_022127, VSP_022128, VSP_022130;
CC Name=3;
CC IsoId=Q9Z173-3; Sequence=VSP_022128, VSP_022130;
CC Name=4; Synonyms=CL3BB;
CC IsoId=Q9Z173-4; Sequence=VSP_022128, VSP_022129, VSP_022132;
CC Name=5; Synonyms=CL3AB;
CC IsoId=Q9Z173-5; Sequence=VSP_022127, VSP_022128, VSP_022129,
CC VSP_022132;
CC Name=6; Synonyms=CL3BC;
CC IsoId=Q9Z173-6; Sequence=VSP_022128, VSP_022131, VSP_022133;
CC Name=7; Synonyms=CL3AC;
CC IsoId=Q9Z173-7; Sequence=VSP_022127, VSP_022128, VSP_022131,
CC VSP_022133;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain, followed by
CC heart, placenta, pancreas, kidney and testis.
CC {ECO:0000269|PubMed:10026162}.
CC -!- DOMAIN: The Olfactomedin-like domain is required for the synapse-
CC promoting function and the interaction with FLRT3. The Olfactomedin-
CC like and the SUEL-type lectin domains are required for the interaction
CC with TENM1 (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000250}.
CC -!- PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AF081154; AAC62660.1; -; mRNA.
DR EMBL; AF081155; AAC62661.1; -; mRNA.
DR EMBL; AF081156; AAC62662.1; -; mRNA.
DR EMBL; AF081157; AAC62663.1; -; mRNA.
DR EMBL; AF081158; AAC62664.1; -; mRNA.
DR EMBL; AF081159; AAC62665.1; -; mRNA.
DR EMBL; AF063103; AAC77816.1; -; mRNA.
DR PIR; T14327; T14327.
DR PIR; T17186; T17186.
DR PIR; T17187; T17187.
DR PIR; T17188; T17188.
DR PIR; T17198; T17198.
DR PIR; T17199; T17199.
DR PIR; T17200; T17200.
DR RefSeq; NP_570835.1; NM_130822.1.
DR AlphaFoldDB; Q9Z173; -.
DR SMR; Q9Z173; -.
DR BioGRID; 250970; 1.
DR STRING; 10116.ENSRNOP00000045365; -.
DR GuidetoPHARMACOLOGY; 208; -.
DR MEROPS; P02.011; -.
DR GlyCosmos; Q9Z173; 8 sites, No reported glycans.
DR GlyGen; Q9Z173; 8 sites.
DR iPTMnet; Q9Z173; -.
DR PhosphoSitePlus; Q9Z173; -.
DR PaxDb; 10116-ENSRNOP00000056687; -.
DR Ensembl; ENSRNOT00055027376; ENSRNOP00055021995; ENSRNOG00055016072. [Q9Z173-1]
DR Ensembl; ENSRNOT00060022218; ENSRNOP00060017605; ENSRNOG00060012994. [Q9Z173-1]
DR Ensembl; ENSRNOT00065007861; ENSRNOP00065005477; ENSRNOG00065005299. [Q9Z173-1]
DR GeneID; 170641; -.
DR KEGG; rno:170641; -.
DR AGR; RGD:620836; -.
DR CTD; 23284; -.
DR RGD; 620836; Adgrl3.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR InParanoid; Q9Z173; -.
DR OrthoDB; 1114672at2759; -.
DR PhylomeDB; Q9Z173; -.
DR PRO; PR:Q9Z173; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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 GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; ISO:RGD.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR CDD; cd16005; 7tmB2_Latrophilin-3; 1.
DR CDD; cd22846; Gal_Rha_Lectin_LPHN3; 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:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 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; 2.
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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1550
FT /note="Adhesion G protein-coupled receptor L3"
FT /id="PRO_0000270141"
FT TOPO_DOM 20..948
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..969
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 978..998
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1006
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1027
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1049..1069
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1070..1087
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1088..1108
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1109..1141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1162
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1163..1168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1169..1189
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1190..1550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 103..192
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 202..461
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 882..933
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 34..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..347
FT /note="Interaction with FLRT3"
FT /evidence="ECO:0000250|UniProtKB:Q9HAR2"
FT REGION 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..134
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 113..191
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 146..178
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 159..165
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT DISULFID 203..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 19..86
FT /note="Missing (in isoform 2, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022127"
FT VAR_SEQ 1131..1139
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022128"
FT VAR_SEQ 1271..1307
FT /note="GSYLPCIQACVTYLEGLLNNARDTSVMDTLPLNGNHG -> EPYRETSMGVK
FT LNIAYQIGASEQCQGYKCHGYSTTEW (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022129"
FT VAR_SEQ 1271..1284
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022130"
FT VAR_SEQ 1272..1350
FT /note="SYLPCIQACVTYLEGLLNNARDTSVMDTLPLNGNHGNSYSIAGGEYLSNCVQ
FT IIDRGYNHNETALEKKILKELTSNYIP -> TMANHLMSNALLRPHGTNNPYNTLLGEP
FT AVCNNPSISMYNAQEPYRETSMGVKLNIAYQIGASEQCQGYKCHGYSTTEW (in
FT isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022131"
FT VAR_SEQ 1308..1550
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022132"
FT VAR_SEQ 1351..1550
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:9830014"
FT /id="VSP_022133"
SQ SEQUENCE 1550 AA; 172442 MW; A2E8091B2B34DB36 CRC64;
MCPPQLFILM MLLAPVVHGG KHNERHPALA APLRHAEHSP GGPLPPRHLL QQPAAERSTA
HRGQGPRGTA RGVRGPGAPG AQIAAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYKVEQKV FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM
PWTPYRTDTL TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN GKIVISQLNP
YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN EATGNKIDYI YNTDQSKDSL
VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY HVVKYSLDFG PLDSRSGPVH HGQVSYISPP
IHLDSDLERP PVRGISTTGP LGMGSTTTST TLRTTTWNLG RSTTPSLPGR RNRSTSTPSP
AIEVLDVTTH LPSAASQIPA MEESCEAVEA REIMWFKTRQ GQVAKQSCPA GTIGVSTYLC
LAPDGIWDPQ GPDLSNCSSP WVNHITQKLK SGETAANIAR ELAEQTRNHL NAGDITYSVR
AMDQLVGLLD VQLRNLTPGG KDSAARSLNK LQKRERSCRA YVQAMVETVN NLLQPQALNA
WRDLTTSDQL RAATMLLDTV EESAFVLADN LLKTDIVREN TDNIQLEVAR LSTEGNLEDL
KFPENTGHGS TIQLSANTLK QNGRNGEIRV AFVLYNNLGP YLSTENASMK LGTEAMSTNH
SVIVNSPVIT AAINKEFSNK VYLADPVVFT VKHIKQSEEN FNPNCSFWSY SKRTMTGYWS
TQGCRLLTTN KTHTTCSCNH LTNFAVLMAH VEVKHSDAVH DLLLDVITWV GILLSLVCLL
ICIFTFCFFR GLQSDRNTIH KNLCISLFVA ELLFLIGINR TDQPIACAVF AALLHFFFLA
AFTWMFLEGV QLYIMLVEVF ESEHSRRKYF YLVGYGMPAL IVAVSAAVDY RSYGTDKVCW
LRLDTYFIWS FIGPATLIIM LNVIFLGIAL YKMFHHTAIL KPESGCLDNI NYEDNRPFIK
SWVIGAIALL CLLGLTWAFG LMYINESTVI MAYLFTIFNS LQGMFIFIFH CVLQKKVRKE
YGKCLRTHCC SGKSTESSIG SGKTSGSRTP GRYSTGSQSR IRRMWNDTVR KQSESSFITG
DINSSASLNR GSYLPCIQAC VTYLEGLLNN ARDTSVMDTL PLNGNHGNSY SIAGGEYLSN
CVQIIDRGYN HNETALEKKI LKELTSNYIP SYLNNHERSS EQNRNMMNKL VDNLGSGSED
DAIVLDDAAS FNHEESLGLE LIHEESDAPL LPPRVYSTDN HQPHHYSRRR LPQDHSESFF
PLLTDEHTED PQSPHRDSLY TSMPALAGVP AADSVTTSTQ TEAAAAKGGD AEDVYYKSMP
NLGSRNHVHP LHAYYQLGRG SSDGFIVPPN KDGASPEGTS KGPAHLVTSL
//
