MEG11_HUMAN
ID MEG11_HUMAN Reviewed; 1044 AA.
AC A6BM72; Q17R86; Q6UXS5; Q8ND91; Q96KG6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 11;
DE Short=Multiple EGF-like domains protein 11;
DE Flags: Precursor;
GN Name=MEGF11; Synonyms=KIAA1781; ORFNames=UNQ1949/PRO4432;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ARG-317 AND PHE-861.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-95 AND
RP ARG-317.
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1044 (ISOFORM 3), AND VARIANT
RP ARG-317.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=17498693; DOI=10.1016/j.yexcr.2007.03.041;
RA Suzuki E., Nakayama M.;
RT "The mammalian Ced-1 ortholog MEGF10/KIAA1780 displays a novel adhesion
RT pattern.";
RL Exp. Cell Res. 313:2451-2464(2007).
CC -!- FUNCTION: May regulate the mosaic spacing of specific neuron subtypes
CC in the retina through homotypic retinal neuron repulsion. Mosaics
CC provide a mechanism to distribute each cell type evenly across the
CC retina, ensuring that all parts of the visual field have access to a
CC full set of processing elements (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomer (Probable). Does not interact with MEGF10.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC A6BM72; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-947743, EBI-1210753;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17498693};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}.
CC Basolateral cell membrane {ECO:0000269|PubMed:17498693}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:17498693}. Note=Forms an
CC irregular, mosaic-like adhesion pattern in region of the cell that
CC becomes firmely fixed to the substrate. Localized to protruding
CC lamellipodia. Does not localize with MEGF10.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A6BM72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6BM72-2; Sequence=VSP_029247, VSP_029248;
CC Name=3;
CC IsoId=A6BM72-3; Sequence=VSP_029249, VSP_029250;
CC Name=4;
CC IsoId=A6BM72-4; Sequence=VSP_029246, VSP_029251, VSP_029252;
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47410.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB058677; BAB47410.2; ALT_INIT; mRNA.
DR EMBL; AB300051; BAF64841.1; -; mRNA.
DR EMBL; AY358226; AAQ88593.1; -; mRNA.
DR EMBL; AC011847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117419; AAI17420.1; -; mRNA.
DR EMBL; BC126313; AAI26314.1; -; mRNA.
DR EMBL; AL834326; CAD38994.1; ALT_INIT; mRNA.
DR CCDS; CCDS10213.2; -. [A6BM72-1]
DR RefSeq; NP_115821.2; NM_032445.2. [A6BM72-1]
DR RefSeq; XP_016878161.1; XM_017022672.1. [A6BM72-1]
DR AlphaFoldDB; A6BM72; -.
DR SMR; A6BM72; -.
DR BioGRID; 124098; 5.
DR IntAct; A6BM72; 3.
DR MINT; A6BM72; -.
DR STRING; 9606.ENSP00000386908; -.
DR GlyGen; A6BM72; 2 sites.
DR iPTMnet; A6BM72; -.
DR PhosphoSitePlus; A6BM72; -.
DR BioMuta; MEGF11; -.
DR MassIVE; A6BM72; -.
DR PaxDb; A6BM72; -.
DR PeptideAtlas; A6BM72; -.
DR PRIDE; A6BM72; -.
DR ProteomicsDB; 769; -. [A6BM72-1]
DR ProteomicsDB; 770; -. [A6BM72-2]
DR ProteomicsDB; 771; -. [A6BM72-3]
DR TopDownProteomics; A6BM72-3; -. [A6BM72-3]
DR Antibodypedia; 42885; 64 antibodies from 14 providers.
DR DNASU; 84465; -.
DR Ensembl; ENST00000288745.7; ENSP00000288745.3; ENSG00000157890.19. [A6BM72-2]
DR Ensembl; ENST00000409699.6; ENSP00000386908.2; ENSG00000157890.19. [A6BM72-1]
DR Ensembl; ENST00000422354.6; ENSP00000414475.1; ENSG00000157890.19. [A6BM72-1]
DR GeneID; 84465; -.
DR KEGG; hsa:84465; -.
DR UCSC; uc002apl.2; human. [A6BM72-1]
DR CTD; 84465; -.
DR DisGeNET; 84465; -.
DR GeneCards; MEGF11; -.
DR HGNC; HGNC:29635; MEGF11.
DR HPA; ENSG00000157890; Tissue enhanced (brain, fallopian tube, kidney, retina).
DR MIM; 612454; gene.
DR neXtProt; NX_A6BM72; -.
DR OpenTargets; ENSG00000157890; -.
DR PharmGKB; PA144596411; -.
DR VEuPathDB; HostDB:ENSG00000157890; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000155333; -.
DR HOGENOM; CLU_008281_1_0_1; -.
DR InParanoid; A6BM72; -.
DR OMA; CGKEAHF; -.
DR OrthoDB; 561378at2759; -.
DR PhylomeDB; A6BM72; -.
DR TreeFam; TF332598; -.
DR PathwayCommons; A6BM72; -.
DR SignaLink; A6BM72; -.
DR BioGRID-ORCS; 84465; 12 hits in 1058 CRISPR screens.
DR ChiTaRS; MEGF11; human.
DR GenomeRNAi; 84465; -.
DR Pharos; A6BM72; Tdark.
DR PRO; PR:A6BM72; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; A6BM72; protein.
DR Bgee; ENSG00000157890; Expressed in cerebellar hemisphere and 114 other tissues.
DR ExpressionAtlas; A6BM72; baseline and differential.
DR Genevisible; A6BM72; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF00053; Laminin_EGF; 7.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 16.
DR PROSITE; PS00022; EGF_1; 17.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1044
FT /note="Multiple epidermal growth factor-like domains
FT protein 11"
FT /id="PRO_0000309735"
FT TOPO_DOM 20..848
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 870..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..101
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 95..130
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 143..173
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 181..216
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 224..259
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 267..302
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 310..345
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 399..434
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 442..477
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 490..520
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 571..606
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 659..694
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 707..737
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 750..780
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 788..823
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1023..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..89
FT /evidence="ECO:0000255"
FT DISULFID 54..63
FT /evidence="ECO:0000255"
FT DISULFID 88..99
FT /evidence="ECO:0000255"
FT DISULFID 103..118
FT /evidence="ECO:0000250"
FT DISULFID 120..129
FT /evidence="ECO:0000250"
FT DISULFID 146..154
FT /evidence="ECO:0000250"
FT DISULFID 148..161
FT /evidence="ECO:0000250"
FT DISULFID 163..172
FT /evidence="ECO:0000250"
FT DISULFID 185..197
FT /evidence="ECO:0000250"
FT DISULFID 191..204
FT /evidence="ECO:0000250"
FT DISULFID 206..215
FT /evidence="ECO:0000250"
FT DISULFID 228..240
FT /evidence="ECO:0000250"
FT DISULFID 234..247
FT /evidence="ECO:0000250"
FT DISULFID 249..258
FT /evidence="ECO:0000250"
FT DISULFID 271..283
FT /evidence="ECO:0000250"
FT DISULFID 277..290
FT /evidence="ECO:0000250"
FT DISULFID 292..301
FT /evidence="ECO:0000250"
FT DISULFID 314..326
FT /evidence="ECO:0000250"
FT DISULFID 320..333
FT /evidence="ECO:0000250"
FT DISULFID 335..344
FT /evidence="ECO:0000250"
FT DISULFID 403..415
FT /evidence="ECO:0000250"
FT DISULFID 409..422
FT /evidence="ECO:0000250"
FT DISULFID 424..433
FT /evidence="ECO:0000250"
FT DISULFID 446..458
FT /evidence="ECO:0000250"
FT DISULFID 452..465
FT /evidence="ECO:0000250"
FT DISULFID 467..476
FT /evidence="ECO:0000250"
FT DISULFID 493..501
FT /evidence="ECO:0000250"
FT DISULFID 495..508
FT /evidence="ECO:0000250"
FT DISULFID 510..519
FT /evidence="ECO:0000250"
FT DISULFID 575..587
FT /evidence="ECO:0000250"
FT DISULFID 581..594
FT /evidence="ECO:0000250"
FT DISULFID 596..605
FT /evidence="ECO:0000250"
FT DISULFID 663..675
FT /evidence="ECO:0000250"
FT DISULFID 669..682
FT /evidence="ECO:0000250"
FT DISULFID 684..693
FT /evidence="ECO:0000250"
FT DISULFID 710..718
FT /evidence="ECO:0000250"
FT DISULFID 712..725
FT /evidence="ECO:0000250"
FT DISULFID 727..736
FT /evidence="ECO:0000250"
FT DISULFID 753..761
FT /evidence="ECO:0000250"
FT DISULFID 755..768
FT /evidence="ECO:0000250"
FT DISULFID 770..779
FT /evidence="ECO:0000250"
FT DISULFID 792..804
FT /evidence="ECO:0000250"
FT DISULFID 798..811
FT /evidence="ECO:0000250"
FT DISULFID 813..822
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..827
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_029246"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_029247"
FT VAR_SEQ 76..101
FT /note="RGLRTMYRRRSQCCPGYYESGDFCIP -> MHTPSIRSITHDAQTSSTGSSA
FT PGTA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_029248"
FT VAR_SEQ 740..875
FT /note="CPAAFFGKDCGRVCQCQNGASCDHISGKCTCRTGFTGQHCEQRCAPGTFGYG
FT CQQLCECMNNSTCDHVTGTCYCSPGFKGIRCDQAALMMEELNPYTKISPALGAERHSVG
FT AVTGIMLLLFLIVVLLGLFAWHRRR -> KPHLLASQPLRIPCCGLLATVGIVQTSREG
FT GMQAAPGLVVPDSCPTRTEELCRGSSRPDWIQGIDKPKVLEGQGCKAAQQHFLGRTVGA
FT YASVRMAPAVTTSVASAPAAQASPGNTVSRDVPQEPLAMGVSSYVSA (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029249"
FT VAR_SEQ 876..1044
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_029250"
FT VAR_SEQ 904..964
FT /note="GACGMDRRQNTYIMDKGFKDYMKESVCSSSTCSLNSSENPYATIKDPPILTC
FT KLPESSYVE -> ASTTPWWPVMEHLARPFSQRPRTQLSNKSLDRDTAGWTPYSYVNVL
FT DQCPGGQVPARGLLH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_029251"
FT VAR_SEQ 965..1044
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_029252"
FT VARIANT 95
FT /note="S -> N (in dbSNP:rs16949528)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059261"
FT VARIANT 242
FT /note="H -> R (in dbSNP:rs333550)"
FT /id="VAR_036990"
FT VARIANT 317
FT /note="H -> R (in dbSNP:rs333550)"
FT /evidence="ECO:0000269|PubMed:11347906,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_059262"
FT VARIANT 474
FT /note="L -> P (in dbSNP:rs35309197)"
FT /id="VAR_059263"
FT VARIANT 861
FT /note="L -> F (in dbSNP:rs3803414)"
FT /evidence="ECO:0000269|PubMed:11347906"
FT /id="VAR_059264"
FT VARIANT 988
FT /note="I -> T (in dbSNP:rs2303374)"
FT /id="VAR_059265"
SQ SEQUENCE 1044 AA; 110844 MW; 8F4CF00B8B1DFCA2 CRC64;
MVLSLTGLIA FSFLQATLAL NPEDPNVCSH WESYAVTVQE SYAHPFDQIY YTRCTDILNW
FKCTRHRISY KTAYRRGLRT MYRRRSQCCP GYYESGDFCI PLCTEECVHG RCVSPDTCHC
EPGWGGPDCS SGCDSDHWGP HCSNRCQCQN GALCNPITGA CVCAAGFRGW RCEELCAPGT
HGKGCQLPCQ CRHGASCDPR AGECLCAPGY TGVYCEELCP PGSHGAHCEL RCPCQNGGTC
HHITGECACP PGWTGAVCAQ PCPPGTFGQN CSQDCPCHHG GQCDHVTGQC HCTAGYMGDR
CQEECPFGSF GFQCSQHCDC HNGGQCSPTT GACECEPGYK GPRCQERLCP EGLHGPGCTL
PCPCDADNTI SCHPVTGACT CQPGWSGHHC NESCPVGYYG DGCQLPCTCQ NGADCHSITG
GCTCAPGFMG EVCAVSCAAG TYGPNCSSIC SCNNGGTCSP VDGSCTCKEG WQGLDCTLPC
PSGTWGLNCN ESCTCANGAA CSPIDGSCSC TPGWLGDTCE LPCPDGTFGL NCSEHCDCSH
ADGCDPVTGH CCCLAGWTGI RCDSTCPPGR WGPNCSVSCS CENGGSCSPE DGSCECAPGF
RGPLCQRICP PGFYGHGCAQ PCPLCVHSSR PCHHISGICE CLPGFSGALC NQVCAGGYFG
QDCAQLCSCA NNGTCSPIDG SCQCFPGWIG KDCSQACPPG FWGPACFHAC SCHNGASCSA
EDGACHCTPG WTGLFCTQRC PAAFFGKDCG RVCQCQNGAS CDHISGKCTC RTGFTGQHCE
QRCAPGTFGY GCQQLCECMN NSTCDHVTGT CYCSPGFKGI RCDQAALMME ELNPYTKISP
ALGAERHSVG AVTGIMLLLF LIVVLLGLFA WHRRRQKEKG RDLAPRVSYT PAMRMTSTDY
SLSGACGMDR RQNTYIMDKG FKDYMKESVC SSSTCSLNSS ENPYATIKDP PILTCKLPES
SYVEMKSPVH MGSPYTDVPS LSTSNKNIYE VEPTVSVVQE GCGHNSSYIQ NAYDLPRNSH
IPGHYDLLPV RQSPANGPSQ DKQS
