AGRL4_HUMAN
ID AGRL4_HUMAN Reviewed; 690 AA.
AC Q9HBW9; B1AR71; Q5KU34;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Adhesion G protein-coupled receptor L4 {ECO:0000303|PubMed:25713288};
DE AltName: Full=EGF, latrophilin and seven transmembrane domain-containing protein 1;
DE AltName: Full=EGF-TM7-latrophilin-related protein;
DE Short=ETL protein;
DE Flags: Precursor;
GN Name=ADGRL4 {ECO:0000303|PubMed:25713288}; Synonyms=ELTD1, ETL;
GN ORFNames=UNQ202/PRO228;
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], AND VARIANT GLY-620.
RC TISSUE=Bone marrow;
RA Hirose M., Urakawa I., Yamano S., Okazaki H.;
RT "Probable G-protein coupled receptor.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-300.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-300.
RC TISSUE=Pancreas;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 67-690, VARIANT LEU-300, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11050079; DOI=10.1074/jbc.m004814200;
RA Nechiporuk T., Urness L.D., Keating M.T.;
RT "ETL, a novel seven-transmembrane receptor that is developmentally
RT regulated in the heart.";
RL J. Biol. Chem. 276:4150-4157(2001).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION, INDUCTION, AND FUNCTION.
RX PubMed=23871637; DOI=10.1016/j.ccr.2013.06.004;
RA Masiero M., Simoes F.C., Han H.D., Snell C., Peterkin T., Bridges E.,
RA Mangala L.S., Wu S.Y., Pradeep S., Li D., Han C., Dalton H.,
RA Lopez-Berestein G., Tuynman J.B., Mortensen N., Li J.L., Patient R.,
RA Sood A.K., Banham A.H., Harris A.L., Buffa F.M.;
RT "A core human primary tumor angiogenesis signature identifies the
RT endothelial orphan receptor ELTD1 as a key regulator of angiogenesis.";
RL Cancer Cell 24:229-241(2013).
RN [9]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
CC -!- FUNCTION: Endothelial orphan receptor that acts as a key regulator of
CC angiogenesis. {ECO:0000269|PubMed:23871637}.
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:0000250|UniProtKB:Q9ESC1, ECO:0000269|PubMed:23871637}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23871637};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in the majority of epithelial cells in
CC tumor and normal tissues. Expressed also in human umbilical vein
CC endothelial cells. {ECO:0000269|PubMed:23871637}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in the adult heart.
CC {ECO:0000269|PubMed:11050079}.
CC -!- INDUCTION: Up-regulated in tumor endothelial cells. Up-regulated by
CC DLL4. {ECO:0000269|PubMed:23871637}.
CC -!- DOMAIN: The transmembrane domain is not required for cleavage, but it
CC is required for dimer formation. {ECO:0000250|UniProtKB:Q9ESC1}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23871637}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit.
CC {ECO:0000250|UniProtKB:Q9ESC1}.
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=AAG33021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH25721.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB032017; BAD83584.1; -; mRNA.
DR EMBL; AY358360; AAQ88726.1; -; mRNA.
DR EMBL; AC098651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06345.1; -; Genomic_DNA.
DR EMBL; BC025721; AAH25721.1; ALT_INIT; mRNA.
DR EMBL; AF192403; AAG33021.1; ALT_INIT; mRNA.
DR CCDS; CCDS41352.1; -.
DR RefSeq; NP_071442.2; NM_022159.3.
DR AlphaFoldDB; Q9HBW9; -.
DR SMR; Q9HBW9; -.
DR BioGRID; 122076; 2.
DR IntAct; Q9HBW9; 1.
DR STRING; 9606.ENSP00000359778; -.
DR ChEMBL; CHEMBL4523920; -.
DR MEROPS; P02.013; -.
DR TCDB; 9.A.14.6.3; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 1915; 15 N-Linked glycans (4 sites).
DR GlyGen; Q9HBW9; 10 sites, 15 N-linked glycans (4 sites).
DR iPTMnet; Q9HBW9; -.
DR PhosphoSitePlus; Q9HBW9; -.
DR BioMuta; ADGRL4; -.
DR DMDM; 212276505; -.
DR EPD; Q9HBW9; -.
DR MassIVE; Q9HBW9; -.
DR PaxDb; Q9HBW9; -.
DR PeptideAtlas; Q9HBW9; -.
DR PRIDE; Q9HBW9; -.
DR ProteomicsDB; 81602; -.
DR ABCD; Q9HBW9; 1 sequenced antibody.
DR Antibodypedia; 9366; 226 antibodies from 30 providers.
DR DNASU; 64123; -.
DR Ensembl; ENST00000370742.4; ENSP00000359778.3; ENSG00000162618.15.
DR GeneID; 64123; -.
DR KEGG; hsa:64123; -.
DR MANE-Select; ENST00000370742.4; ENSP00000359778.3; NM_022159.4; NP_071442.2.
DR UCSC; uc001diq.5; human.
DR CTD; 64123; -.
DR DisGeNET; 64123; -.
DR GeneCards; ADGRL4; -.
DR HGNC; HGNC:20822; ADGRL4.
DR HPA; ENSG00000162618; Tissue enhanced (adipose).
DR MIM; 616419; gene.
DR neXtProt; NX_Q9HBW9; -.
DR OpenTargets; ENSG00000162618; -.
DR PharmGKB; PA134946418; -.
DR VEuPathDB; HostDB:ENSG00000162618; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000158252; -.
DR HOGENOM; CLU_002753_3_8_1; -.
DR InParanoid; Q9HBW9; -.
DR OMA; SKMKHIH; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q9HBW9; -.
DR TreeFam; TF316380; -.
DR PathwayCommons; Q9HBW9; -.
DR SignaLink; Q9HBW9; -.
DR BioGRID-ORCS; 64123; 10 hits in 1071 CRISPR screens.
DR GeneWiki; ELTD1; -.
DR GenomeRNAi; 64123; -.
DR Pharos; Q9HBW9; Tbio.
DR PRO; PR:Q9HBW9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HBW9; protein.
DR Bgee; ENSG00000162618; Expressed in pericardium and 186 other tissues.
DR ExpressionAtlas; Q9HBW9; baseline and differential.
DR Genevisible; Q9HBW9; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR032471; GAIN_dom_N.
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; PF07645; EGF_CA; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 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 Calcium; Cell membrane; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..690
FT /note="Adhesion G protein-coupled receptor L4"
FT /id="PRO_0000012870"
FT TOPO_DOM 20..432
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..481
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..499
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 500..520
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 533..553
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..573
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 574..594
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 619..639
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..646
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 647..667
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..57
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 58..108
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 367..418
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 406..407
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9ESC1"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
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 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..33
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 27..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 44..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 62..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 69..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 86..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 300
FT /note="V -> L (in dbSNP:rs12754818)"
FT /evidence="ECO:0000269|PubMed:11050079,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334"
FT /id="VAR_047072"
FT VARIANT 599
FT /note="H -> Q (in dbSNP:rs1968956)"
FT /id="VAR_047073"
FT VARIANT 620
FT /note="A -> G (in dbSNP:rs2275902)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_047074"
SQ SEQUENCE 690 AA; 77811 MW; 38BFEEBCEADDEFC8 CRC64;
MKRLPLLVVF STLLNCSYTQ NCTKTPCLPN AKCEIRNGIE ACYCNMGFSG NGVTICEDDN
ECGNLTQSCG ENANCTNTEG SYYCMCVPGF RSSSNQDRFI TNDGTVCIEN VNANCHLDNV
CIAANINKTL TKIRSIKEPV ALLQEVYRNS VTDLSPTDII TYIEILAESS SLLGYKNNTI
SAKDTLSNST LTEFVKTVNN FVQRDTFVVW DKLSVNHRRT HLTKLMHTVE QATLRISQSF
QKTTEFDTNS TDIALKVFFF DSYNMKHIHP HMNMDGDYIN IFPKRKAAYD SNGNVAVAFV
YYKSIGPLLS SSDNFLLKPQ NYDNSEEEER VISSVISVSM SSNPPTLYEL EKITFTLSHR
KVTDRYRSLC AFWNYSPDTM NGSWSSEGCE LTYSNETHTS CRCNHLTHFA ILMSSGPSIG
IKDYNILTRI TQLGIIISLI CLAICIFTFW FFSEIQSTRT TIHKNLCCSL FLAELVFLVG
INTNTNKLFC SIIAGLLHYF FLAAFAWMCI EGIHLYLIVV GVIYNKGFLH KNFYIFGYLS
PAVVVGFSAA LGYRYYGTTK VCWLSTENNF IWSFIGPACL IILVNLLAFG VIIYKVFRHT
AGLKPEVSCF ENIRSCARGA LALLFLLGTT WIFGVLHVVH ASVVTAYLFT VSNAFQGMFI
FLFLCVLSRK IQEEYYRLFK NVPCCFGCLR
