WDTC1_HUMAN
ID WDTC1_HUMAN Reviewed; 677 AA.
AC Q8N5D0; D3DPL5; Q5SSC5; Q9NV87; Q9UPW4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=WD and tetratricopeptide repeats protein 1;
GN Name=WDTC1; Synonyms=KIAA1037;
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).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lymph;
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 110-677 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP FUNCTION.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase
RT machinery.";
RL Nature 443:590-593(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16964240}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q8N5D0-4; Q16531: DDB1; NbExp=3; IntAct=EBI-15821254, EBI-350322;
CC Q8N5D0-4; P40337-2: VHL; NbExp=3; IntAct=EBI-15821254, EBI-12157263;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8N5D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5D0-2; Sequence=VSP_009292;
CC Name=3;
CC IsoId=Q8N5D0-3; Sequence=VSP_009291;
CC Name=4;
CC IsoId=Q8N5D0-4; Sequence=VSP_009290;
CC Name=5;
CC IsoId=Q8N5D0-5; Sequence=VSP_009290, VSP_009291;
CC Name=6;
CC IsoId=Q8N5D0-6; Sequence=VSP_009290, VSP_009292;
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DR EMBL; AK001734; BAA91868.1; -; mRNA.
DR EMBL; AL590640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07770.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07771.1; -; Genomic_DNA.
DR EMBL; BC032523; AAH32523.1; -; mRNA.
DR EMBL; AB028960; BAA82989.1; -; mRNA.
DR CCDS; CCDS296.1; -. [Q8N5D0-4]
DR CCDS; CCDS60044.1; -. [Q8N5D0-1]
DR RefSeq; NP_001263181.1; NM_001276252.1. [Q8N5D0-1]
DR RefSeq; NP_055838.2; NM_015023.4. [Q8N5D0-4]
DR RefSeq; XP_011539359.1; XM_011541057.1. [Q8N5D0-1]
DR PDB; 3I7N; X-ray; 2.80 A; B=5-17.
DR PDBsum; 3I7N; -.
DR AlphaFoldDB; Q8N5D0; -.
DR SMR; Q8N5D0; -.
DR BioGRID; 116677; 87.
DR DIP; DIP-31627N; -.
DR IntAct; Q8N5D0; 31.
DR STRING; 9606.ENSP00000317971; -.
DR iPTMnet; Q8N5D0; -.
DR MetOSite; Q8N5D0; -.
DR PhosphoSitePlus; Q8N5D0; -.
DR BioMuta; WDTC1; -.
DR DMDM; 41018470; -.
DR EPD; Q8N5D0; -.
DR jPOST; Q8N5D0; -.
DR MassIVE; Q8N5D0; -.
DR MaxQB; Q8N5D0; -.
DR PaxDb; Q8N5D0; -.
DR PeptideAtlas; Q8N5D0; -.
DR PRIDE; Q8N5D0; -.
DR ProteomicsDB; 72037; -. [Q8N5D0-1]
DR ProteomicsDB; 72038; -. [Q8N5D0-2]
DR ProteomicsDB; 72039; -. [Q8N5D0-3]
DR ProteomicsDB; 72040; -. [Q8N5D0-4]
DR ProteomicsDB; 72041; -. [Q8N5D0-5]
DR ProteomicsDB; 72042; -. [Q8N5D0-6]
DR Antibodypedia; 30730; 131 antibodies from 20 providers.
DR DNASU; 23038; -.
DR Ensembl; ENST00000319394.8; ENSP00000317971.3; ENSG00000142784.16. [Q8N5D0-1]
DR Ensembl; ENST00000361771.7; ENSP00000355317.3; ENSG00000142784.16. [Q8N5D0-4]
DR Ensembl; ENST00000447062.2; ENSP00000434578.1; ENSG00000142784.16. [Q8N5D0-2]
DR GeneID; 23038; -.
DR KEGG; hsa:23038; -.
DR MANE-Select; ENST00000319394.8; ENSP00000317971.3; NM_001276252.2; NP_001263181.1.
DR UCSC; uc001bno.5; human. [Q8N5D0-1]
DR CTD; 23038; -.
DR DisGeNET; 23038; -.
DR GeneCards; WDTC1; -.
DR HGNC; HGNC:29175; WDTC1.
DR HPA; ENSG00000142784; Low tissue specificity.
DR MIM; 619763; gene.
DR neXtProt; NX_Q8N5D0; -.
DR OpenTargets; ENSG00000142784; -.
DR PharmGKB; PA134981539; -.
DR VEuPathDB; HostDB:ENSG00000142784; -.
DR eggNOG; KOG1310; Eukaryota.
DR eggNOG; KOG1334; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_012381_3_1_1; -.
DR InParanoid; Q8N5D0; -.
DR OMA; HWQRQQY; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q8N5D0; -.
DR TreeFam; TF320710; -.
DR PathwayCommons; Q8N5D0; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q8N5D0; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 23038; 53 hits in 1126 CRISPR screens.
DR ChiTaRS; WDTC1; human.
DR EvolutionaryTrace; Q8N5D0; -.
DR GenomeRNAi; 23038; -.
DR Pharos; Q8N5D0; Tbio.
DR PRO; PR:Q8N5D0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N5D0; protein.
DR Bgee; ENSG00000142784; Expressed in hindlimb stylopod muscle and 196 other tissues.
DR ExpressionAtlas; Q8N5D0; baseline and differential.
DR Genevisible; Q8N5D0; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0055082; P:cellular chemical homeostasis; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..677
FT /note="WD and tetratricopeptide repeats protein 1"
FT /id="PRO_0000051434"
FT REPEAT 45..84
FT /note="WD 1"
FT REPEAT 88..129
FT /note="WD 2"
FT REPEAT 132..172
FT /note="WD 3"
FT REPEAT 182..222
FT /note="WD 4"
FT REPEAT 265..305
FT /note="WD 5"
FT REPEAT 362..395
FT /note="TPR 1"
FT REPEAT 397..432
FT /note="TPR 2"
FT REPEAT 535..575
FT /note="WD 6"
FT REPEAT 578..617
FT /note="WD 7"
FT REGION 487..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 317
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009290"
FT VAR_SEQ 548..677
FT /note="SNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSG
FT IDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNADPLEVMLLNMGYRITGLSSGG
FT AGASDDEDSSEGQVQCRPS -> RRPPTWSVCSKGMSPLSTACSHTPATASWPPVASIL
FT LCGSGTPDQRVKTSQAESWKIWRVLHRPTSGA (in isoform 2 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009292"
FT VAR_SEQ 548..677
FT /note="SNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSG
FT IDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNADPLEVMLLNMGYRITGLSSGG
FT AGASDDEDSSEGQVQCRPS -> RSEALKRRVQPSWQREVEWGVLGHNGFREESQIPAL
FT PLYPWANGFTFVSL (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10470851"
FT /id="VSP_009291"
FT CONFLICT 456
FT /note="L -> P (in Ref. 1; BAA91868)"
FT /evidence="ECO:0000305"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:3I7N"
SQ SEQUENCE 677 AA; 75920 MW; 2BDFA8061B2C266C CRC64;
MAKVNITRDL IRRQIKERGA LSFERRYHVT DPFIRRLGLE AELQGHSGCV NCLEWNEKGD
LLASGSDDQH TIVWDPLHHK KLLSMHTGHT ANIFSVKFLP HAGDRILITG AADSKVHVHD
LTVKETIHMF GDHTNRVKRI ATAPMWPNTF WSAAEDGLIR QYDLRENSKH SEVLIDLTEY
CGQLVEAKCL TVNPQDNNCL AVGASGPFVR LYDIRMIHNH RKSMKQSPSA GVHTFCDRQK
PLPDGAAQYY VAGHLPVKLP DYNNRLRVLV ATYVTFSPNG TELLVNMGGE QVYLFDLTYK
QRPYTFLLPR KCHSSGEVQN GKMSTNGVSN GVSNGLHLHS NGFRLPESRG HVSPQVELPP
YLERVKQQAN EAFACQQWTQ AIQLYSKAVQ RAPHNAMLYG NRAAAYMKRK WDGDHYDALR
DCLKAISLNP CHLKAHFRLA RCLFELKYVA EALECLDDFK GKFPEQAHSS ACDALGRDIT
AALFSKNDGE EKKGPGGGAP VRLRSTSRKD SISEDEMVLR ERSYDYQFRY CGHCNTTTDI
KEANFFGSNA QYIVSGSDDG SFFIWEKETT NLVRVLQGDE SIVNCLQPHP SYCFLATSGI
DPVVRLWNPR PESEDLTGRV VEDMEGASQA NQRRMNADPL EVMLLNMGYR ITGLSSGGAG
ASDDEDSSEG QVQCRPS
