ELAP1_HUMAN
ID ELAP1_HUMAN Reviewed; 1013 AA.
AC Q6UXG2; Q08AE6; Q5T5C9; Q5T5D0; Q5T5D1; Q9P2M2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Endosome/lysosome-associated apoptosis and autophagy regulator 1 {ECO:0000305};
DE AltName: Full=Estrogen-induced gene 121 protein {ECO:0000303|PubMed:16322283};
DE Flags: Precursor;
GN Name=ELAPOR1 {ECO:0000312|HGNC:HGNC:29618};
GN Synonyms=EIG121 {ECO:0000303|PubMed:16322283},
GN KIAA1324 {ECO:0000312|EMBL:BAA92562.1};
GN ORFNames=UNQ2426/PRO4985 {ECO:0000312|EMBL:AAQ88732.1};
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] (ISOFORM 2), AND VARIANTS VAL-86 AND
RP PRO-623.
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS VAL-86 AND
RP PRO-623 AND PRO-1009.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1013 (ISOFORM 4), AND VARIANT
RP PRO-623.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP IDENTIFICATION, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Endometrium;
RX PubMed=16322283; DOI=10.1158/1078-0432.ccr-05-1189;
RA Deng L., Broaddus R.R., McCampbell A., Shipley G.L., Loose D.S.,
RA Stancel G.M., Pickar J.H., Davies P.J.A.;
RT "Identification of a novel estrogen-regulated gene, EIG121, induced by
RT hormone replacement therapy and differentially expressed in type I and type
RT II endometrial cancer.";
RL Clin. Cancer Res. 11:8258-8264(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21072319; DOI=10.1038/cddis.2010.9;
RA Deng L., Feng J., Broaddus R.R.;
RT "The novel estrogen-induced gene EIG121 regulates autophagy and promotes
RT cell survival under stress.";
RL Cell Death Dis. 1:E32-E32(2010).
RN [7]
RP FUNCTION, INTERACTION WITH HSPA5, AND SUBCELLULAR LOCATION.
RX PubMed=26045166; DOI=10.1158/0008-5472.can-14-3751;
RA Kang J.M., Park S., Kim S.J., Kim H., Lee B., Kim J., Park J., Kim S.T.,
RA Yang H.K., Kim W.H., Kim S.J.;
RT "KIAA1324 Suppresses Gastric Cancer Progression by Inhibiting the
RT Oncoprotein GRP78.";
RL Cancer Res. 75:3087-3097(2015).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-829.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May protect cells from cell death by inducing cytosolic
CC vacuolization and up-regulating the autophagy pathway
CC (PubMed:21072319). May play a role in apoptosis and cell proliferation
CC through its interaction with HSPA5 (PubMed:26045166).
CC {ECO:0000269|PubMed:21072319, ECO:0000269|PubMed:26045166}.
CC -!- SUBUNIT: Interacts with HSPA5; may regulate the function of HSPA5 in
CC apoptosis and cell proliferation. {ECO:0000269|PubMed:26045166}.
CC -!- INTERACTION:
CC Q6UXG2-3; P28329-3: CHAT; NbExp=3; IntAct=EBI-12920100, EBI-25837549;
CC Q6UXG2-3; Q99828: CIB1; NbExp=3; IntAct=EBI-12920100, EBI-372594;
CC Q6UXG2-3; P22607: FGFR3; NbExp=3; IntAct=EBI-12920100, EBI-348399;
CC Q6UXG2-3; P14136: GFAP; NbExp=3; IntAct=EBI-12920100, EBI-744302;
CC Q6UXG2-3; P28799: GRN; NbExp=3; IntAct=EBI-12920100, EBI-747754;
CC Q6UXG2-3; P04792: HSPB1; NbExp=3; IntAct=EBI-12920100, EBI-352682;
CC Q6UXG2-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12920100, EBI-1055254;
CC Q6UXG2-3; P07196: NEFL; NbExp=3; IntAct=EBI-12920100, EBI-475646;
CC Q6UXG2-3; Q9Y649; NbExp=3; IntAct=EBI-12920100, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21072319,
CC ECO:0000269|PubMed:26045166}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21072319}. Late endosome membrane
CC {ECO:0000269|PubMed:21072319}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21072319}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:21072319}; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:21072319}. Lysosome membrane
CC {ECO:0000269|PubMed:21072319}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21072319}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26045166}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:21072319}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6UXG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UXG2-2; Sequence=VSP_025116;
CC Name=3;
CC IsoId=Q6UXG2-3; Sequence=VSP_025115;
CC Name=4;
CC IsoId=Q6UXG2-4; Sequence=VSP_025117;
CC -!- TISSUE SPECIFICITY: Expressed in normal endometrium but overexpressed
CC in endometroid tumors. {ECO:0000269|PubMed:16322283}.
CC -!- INDUCTION: By estrogen replacement therapy.
CC {ECO:0000269|PubMed:16322283}.
CC -!- SIMILARITY: Belongs to the ELAPOR family. {ECO:0000305}.
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DR EMBL; AY358366; AAQ88732.1; -; mRNA.
DR EMBL; AL138933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125208; AAI25209.1; -; mRNA.
DR EMBL; AB037745; BAA92562.1; -; mRNA.
DR CCDS; CCDS58015.1; -. [Q6UXG2-3]
DR CCDS; CCDS794.1; -. [Q6UXG2-1]
DR RefSeq; NP_001253977.1; NM_001267048.1. [Q6UXG2-3]
DR RefSeq; NP_065826.2; NM_020775.4. [Q6UXG2-1]
DR RefSeq; XP_011540127.1; XM_011541825.1. [Q6UXG2-4]
DR AlphaFoldDB; Q6UXG2; -.
DR BioGRID; 121594; 64.
DR IntAct; Q6UXG2; 12.
DR STRING; 9606.ENSP00000358955; -.
DR GlyConnect; 1884; 12 N-Linked glycans (3 sites).
DR GlyGen; Q6UXG2; 8 sites, 12 N-linked glycans (3 sites).
DR iPTMnet; Q6UXG2; -.
DR PhosphoSitePlus; Q6UXG2; -.
DR BioMuta; KIAA1324; -.
DR DMDM; 147647000; -.
DR EPD; Q6UXG2; -.
DR jPOST; Q6UXG2; -.
DR MassIVE; Q6UXG2; -.
DR MaxQB; Q6UXG2; -.
DR PaxDb; Q6UXG2; -.
DR PeptideAtlas; Q6UXG2; -.
DR PRIDE; Q6UXG2; -.
DR ProteomicsDB; 67605; -. [Q6UXG2-1]
DR ProteomicsDB; 67606; -. [Q6UXG2-2]
DR ProteomicsDB; 67607; -. [Q6UXG2-3]
DR ProteomicsDB; 67608; -. [Q6UXG2-4]
DR Antibodypedia; 33748; 183 antibodies from 26 providers.
DR DNASU; 57535; -.
DR Ensembl; ENST00000369939.8; ENSP00000358955.3; ENSG00000116299.17. [Q6UXG2-1]
DR Ensembl; ENST00000529753.5; ENSP00000434595.1; ENSG00000116299.17. [Q6UXG2-3]
DR GeneID; 57535; -.
DR KEGG; hsa:57535; -.
DR MANE-Select; ENST00000369939.8; ENSP00000358955.3; NM_020775.5; NP_065826.3.
DR UCSC; uc009wey.4; human. [Q6UXG2-1]
DR CTD; 57535; -.
DR DisGeNET; 57535; -.
DR GeneCards; ELAPOR1; -.
DR HGNC; HGNC:29618; ELAPOR1.
DR HPA; ENSG00000116299; Tissue enhanced (pancreas, salivary gland, stomach).
DR MIM; 611298; gene.
DR neXtProt; NX_Q6UXG2; -.
DR OpenTargets; ENSG00000116299; -.
DR VEuPathDB; HostDB:ENSG00000116299; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156861; -.
DR HOGENOM; CLU_005066_0_0_1; -.
DR InParanoid; Q6UXG2; -.
DR OMA; RYFHRFN; -.
DR OrthoDB; 192139at2759; -.
DR PhylomeDB; Q6UXG2; -.
DR TreeFam; TF315906; -.
DR PathwayCommons; Q6UXG2; -.
DR SignaLink; Q6UXG2; -.
DR BioGRID-ORCS; 57535; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; KIAA1324; human.
DR GenomeRNAi; 57535; -.
DR Pharos; Q6UXG2; Tbio.
DR PRO; PR:Q6UXG2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6UXG2; protein.
DR Bgee; ENSG00000116299; Expressed in parotid gland and 146 other tissues.
DR ExpressionAtlas; Q6UXG2; baseline and differential.
DR Genevisible; Q6UXG2; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:BHF-UCL.
DR GO; GO:0009267; P:cellular response to starvation; IMP:BHF-UCL.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:BHF-UCL.
DR GO; GO:0044090; P:positive regulation of vacuole organization; IMP:BHF-UCL.
DR InterPro; IPR039181; EIG121-like.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR PANTHER; PTHR22727; PTHR22727; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Lysosome;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1013
FT /note="Endosome/lysosome-associated apoptosis and autophagy
FT regulator 1"
FT /id="PRO_0000286600"
FT TOPO_DOM 42..910
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 932..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 656..858
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 278..295
FT /evidence="ECO:0000250"
FT DISULFID 308..330
FT /evidence="ECO:0000250"
FT DISULFID 311..342
FT /evidence="ECO:0000250"
FT DISULFID 658..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 714..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 808..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 820..856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 261..347
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025115"
FT VAR_SEQ 992..1013
FT /note="RTPDGFDSVPLKTSSGGLDMDL -> FKDS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_025116"
FT VAR_SEQ 992..1013
FT /note="RTPDGFDSVPLKTSSGGLDMDL -> QPAPVTISLSEDS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_025117"
FT VARIANT 86
FT /note="I -> V (in dbSNP:rs678238)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032138"
FT VARIANT 623
FT /note="T -> P (in dbSNP:rs659543)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15489334"
FT /id="VAR_032139"
FT VARIANT 829
FT /note="S -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035751"
FT VARIANT 1009
FT /note="L -> P (in dbSNP:rs1052878)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032140"
FT CONFLICT 239
FT /note="N -> K (in Ref. 3; AAI25209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 111382 MW; 875440C1946582A7 CRC64;
MAEPGHSHHL SARVRGRTER RIPRLWRLLL WAGTAFQVTQ GTGPELHACK ESEYHYEYTA
CDSTGSRWRV AVPHTPGLCT SLPDPIKGTE CSFSCNAGEF LDMKDQSCKP CAEGRYSLGT
GIRFDEWDEL PHGFASLSAN MELDDSAAES TGNCTSSKWV PRGDYIASNT DECTATLMYA
VNLKQSGTVN FEYYYPDSSI IFEFFVQNDQ CQPNADDSRW MKTTEKGWEF HSVELNRGNN
VLYWRTTAFS VWTKVPKPVL VRNIAITGVA YTSECFPCKP GTYADKQGSS FCKLCPANSY
SNKGETSCHQ CDPDKYSEKG SSSCNVRPAC TDKDYFYTHT ACDANGETQL MYKWAKPKIC
SEDLEGAVKL PASGVKTHCP PCNPGFFKTN NSTCQPCPYG SYSNGSDCTR CPAGTEPAVG
FEYKWWNTLP TNMETTVLSG INFEYKGMTG WEVAGDHIYT AAGASDNDFM ILTLVVPGFR
PPQSVMADTE NKEVARITFV FETLCSVNCE LYFMVGVNSR TNTPVETWKG SKGKQSYTYI
IEENTTTSFT WAFQRTTFHE ASRKYTNDVA KIYSINVTNV MNGVASYCRP CALEASDVGS
SCTSCPAGYY IDRDSGTCHS CPTNTILKAH QPYGVQACVP CGPGTKNNKI HSLCYNDCTF
SRNTPTRTFN YNFSALANTV TLAGGPSFTS KGLKYFHHFT LSLCGNQGRK MSVCTDNVTD
LRIPEGESGF SKSITAYVCQ AVIIPPEVTG YKAGVSSQPV SLADRLIGVT TDMTLDGITS
PAELFHLESL GIPDVIFFYR SNDVTQSCSS GRSTTIRVRC SPQKTVPGSL LLPGTCSDGT
CDGCNFHFLW ESAAACPLCS VADYHAIVSS CVAGIQKTTY VWREPKLCSG GISLPEQRVT
ICKTIDFWLK VGISAGTCTA ILLTVLTCYF WKKNQKLEYK YSKLVMNATL KDCDLPAADS
CAIMEGEDVE DDLIFTSKKS LFGKIKSFTS KRTPDGFDSV PLKTSSGGLD MDL
