ID G1L6L1_AILME Unreviewed; 4861 AA.
AC G1L6L1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=HECT and RLD domain containing E3 ubiquitin protein ligase family member 1 {ECO:0000313|Ensembl:ENSAMEP00000002526.2};
GN Name=HERC1 {ECO:0000313|Ensembl:ENSAMEP00000002526.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002526.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002526.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002526.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_002914279.1; XM_002914233.3.
DR STRING; 9646.ENSAMEP00000002526; -.
DR Ensembl; ENSAMET00000002636.2; ENSAMEP00000002526.2; ENSAMEG00000002389.2.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000155907; -.
DR HOGENOM; CLU_000091_0_0_1; -.
DR InParanoid; G1L6L1; -.
DR TreeFam; TF106426; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd12881; SPRY_HERC1; 1.
DR CDD; cd14401; UBA_HERC1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035768; SPRY_HERC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR22872:SF6; E3 UBIQUITIN-PROTEIN LIGASE HERC1-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 10.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00449; SPRY; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00626; RCC1_2; 4.
DR PROSITE; PS50012; RCC1_3; 14.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 372..421
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 422..476
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 477..529
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 530..579
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 581..632
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 633..683
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 684..736
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 2002..2193
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REPEAT 3424..3465
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 3622..3653
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 3743..3784
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 3997..4045
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4046..4100
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4101..4152
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4153..4204
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4206..4257
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4258..4309
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4310..4361
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 4501..4848
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 125..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2257..2288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2407..2462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2475..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2617..2675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2692..2752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2798..2876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3235..3255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2407..2436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2447..2462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2480..2494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2622..2669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2692..2743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3235..3250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4811
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4861 AA; 531359 MW; D691569AF48DA521 CRC64;
MATMVPPVKL KWLEHLNSSW ITEDSESIAT REGVAVLYSK LVSNKEVVPL PQQVLCLKGP
QLPDFERESL SSDEQDHYLD ALLSSQLALA KMVCSDSPFA GALRKRLLVL QRVFYALSNK
YHDKGKVKQQ QHSPESSSGS ADVHSVSERP RSSTDALIEM GVRTGLSLLF ALLRQSWMMP
VSGPGLSLCN DVIHTAIEVV SSLPPLSLAN ESKIPPMGLD CLSQVTTFLK GVTIPNSGAD
TLGRRLASEL LLGLAAQRGS LRYLLEWIEM ALGASAVVNS MEKSKLLSSQ EGMISFDCFM
TILMQMRRSL GSSADRSQWR EPTRTSDGLC SLYEAALCLF EEVCRMASDY SRTCASPDSI
QTGDAPIVSE TCEVYVWGSN SSHQLVEGTQ EKILQPKLAP SFSDAQTIEA GQYCTFVIST
DGSVRACGKG SYGRLGLGDS NNQSTLKKLT FEPHRSIKKV SSSKGSDGHT LAFTTEGEVF
SWGDGDYGKL GHGNSSTQKY PKLIQGPLQG KVVVCVSAGY RHSAAVTEDG ELYTWGEGDF
GRLGHGDSNS RNIPTLVKDI SNVGEVSCGS SHTIALSKDG RTVWSFGGGD NGKLGHGDTN
RVYKPKVVEA LQGMFIRKVC AGSQSSLALT STGQVYAWGC GACLGCGSSE ATALRPKLIE
ELAATRIVDI SIGDSHCLAL SHDNEVYAWG NNSMGQCGQG NSTGPITKPK KVSGLDGIAI
QQISAGTSHS LAWTALPRDR QVVAWHRPYC VDLEESTFSH LRSFLERYCD KINSEIPPLP
FPSSREHHNF LKLCLKLLSN HLALALAGGV ATSILGRQAG PLRNLLFRLM DSTVPDEIQE
VVIETLSVGA TMLLPPLRER MELLHSLLPQ GPDRWESLSK GQRMQLDIIL TSLQDHTHVA
SLLGYSSPSD AADLSSVCTG YGNLSDQPYG AQSCHPDTHL AEILMKTLLR NLGFYTDQAF
GELEKNSDKF LLGTSSSENS QPAHLHELLC SLQKQLLAFC HINNISENSS SVALLHKHLQ
LLLPHATDIY SRSANLLKES PWNGSVGEKL RDVIYVSAAG SMLCQIVNSL LLLPVSVARP
LLSYLLDLLP PLDCLNRLLP AAALLEDQEL QWPLHGGPEL IDPAGMPLPQ PAQAWVWLVD
LERTIALLIG RCLGGMLLGS PVSPEEQDTA YWMKTPLFSD GVEMDTPQLD KCMSCLLEVA
LSGNEEQKPF DYKLRPEIAV YVDLALGCSK EPARSLWISM QDYAVSKDWD SATLSNESLL
DTVSRFVLAA LLKHTNLLSQ ACGESRYQPG KSLSEVYRCV YKVRSRLLAC KNLELIQTRS
SSRDRWISEN QDSADVDPQE CSFARTIDEE AEMEEQAERD REEGHPEPED EEEEREHEVM
TAGKIFQCFL SAREVARSRD RDRMNSGAGS GARADDPPPQ SQQERRVSTD LPEGQDVYTA
ACNSVIHRCA LLILGVSPVI DELQKRKEEG QLQQPSASAT EGGGLMTRSE SLTAESRLVH
ASPNYRLIKS RSESDLSQPE SDEEGYALSG RRNVDLDLAS SHRKRGPLHS QLESLSDSWA
RLKHSRDWLC NSSYSFESDF DLTKSLGVHT LIENVVSFVS GDVGNAPGFK EPEESMSTSP
QASIIAMEQQ QLRAELRLEA LHQILVLLSG MEEKGSISLA GSRSSSGFQS STLLTSVRLQ
FLAGCFGLGT VGHAGAKGES GRLHHYQDGI RAAKRNIQIE IQVAVHKIYQ QLSATLERAL
QANKHHIEAQ QRLLLVTVFA LSVHYQPVDV SLAISTGLLN VLSQLCGTDT MLGQPLQLLP
KTGVSQLSTA LKVASTRLLQ ILAITTGTYA DKLSPKVVQS LLDLLCSQLK NLLSQAGVLL
MASFGEEEGE EGEEEEKKVD SSGETEKKDF RAALRKQHAA ELHLGDFLVF LRRVVSSKAI
QSKMASPKWT EVLLNIASQK CSSGIPLVGN LRTRLLALHV LEAVLPACES GVEDDQMAQV
VERLFSLLSD CMWETPIAQA KHAIQIKEKE QEIKSQKQGD LEEEDENLPI QEVSFDPEKA
QCCLVENGQI LTHGSGGKGY GLASTGVTSG CYQWKFYIVK ENRGNEGTCV GVSRWPVHDF
NHRTTSDMWL YRAYSGNLYH NGEQTLTLSS FTQGDFITCV LDMEARTISF GKNGEEPKLA
FEDVDAAELY PCVMFYSSNP GEKVKICDMQ MRGTPRDLLP GDPICSPVAA VLAEATIQLI
RILHRTDRWT YCINKKMMER LHKIKICIKE SGQKLKKSRS VQSREENEMR EEKESKEEEK
GKHNRHGLAD LSEPQLRTLC IEVWPVLAVI GGVDAGLRVG GRCVHKQTGR HATLLGVVKE
GSTSAKVQWD EAEITISFPT FWSPSDTPLY NLEPCEPLPF DVARFRGLTA SVLLDLTYLT
GIHEDMGKQS TKRHEKKHRH ESEEKGDVEQ KTESESAVDM RVGLTSDDVK SQGTTASKSD
NEIASFSLDS ALPSVESQHQ ITEGKRKNHE HISKNHDIAQ SEIRAVQLSY LYLGAMKSLS
ALLGCSKYAE LLLIPKVLAE NGHNSDCASS PVVHEDVEMR AALQFLMRHM VKRAVMRSPI
KRALGLADLE RAQAMIYKLV VHGLLEDQFG GKIKQEIDQQ AEESDQAQQA QTPVTTSPSA
SSTTSFMSSS LEDTTTATTP VTDTETVPAS ESPGVMPLSL LRQMFSSYPT TTVLPTRRAQ
TPPISSLPTS PSDEVGRRQS LTSPDSQSAR PANRTALSDP SSRLSTSPPP PAIAVPLLEM
GFSLRQIAKA MEATGARGEA DAQNITVLAM WMIEHPGHED EEEPQSGSTA DARPGAAVLG
SGGKSNDPCY LQSPGDIPSA DAAEMEEGFS ESPDNLDHTE NAASGSGPPA RGRSAVTRRH
KFDLAARTLL ARAAGLYRSV QAHRNQSRRE GISLQQDPGA LYDFNLDEEL EIDLDDEAME
AVFGQDLTGD SDILGMWIPE VLDWPTWHVC ESEDREEVVV CELCECSVVS FNQHMKRNHP
GCGRSANRQG YRSNGSYVDG WFGGECGSGN PYYLLCGSCR EKYLALKTKS KTTSSERYKG
QAPDLIGKQD SVYEEDWDML DVDEDEKLTG EEEFELLAGP LGLNDRRIVP EPVQFPDSDP
LGASVAMVTA TNSMEETLMQ IGCHGSVEKS SSGRITLGEQ AAALANPHDR VVALRRVTAA
AQVLLARTMV MRALSLLSVS GSSCSLAAGL ESLGLTDIRT LVRLMCLAAA GRAGLSTSPS
ATASPSERSR GGHSKASKPM SCLAYLSTAV GCLASNTPSA AKLLVQLCTQ NLISAATGVN
LTTVDDPIQR KFLPSFLRGI AEENKLVTSP NFVVTQALVA LLADKGAKLR PNYDKSEVEK
KGPLELANAL AACCLSSRLS SQHRQWAAQQ LVRTLAAHDR DNQTTPQTLA DMGGDLRKCS
FIKLEAHQNR VMTCVWCNKK GLLATSGNDG TIRVWNVTKK QYSLQQTCVF NRLEGDAEES
LGSPSDPSFS PVSWSISGKY LAGALEKMVN IWQVNGGKGL VDIQPHWVSA LAWPEEGPAT
AWSGESPELL LVGRMDGSLG LIEVVDVSTM HRRELEHCYR KDVSVTCIAW FSEDRPFAVG
YFDGKLLLGT KEPLEKGGIV LIDAHKDTLV SMKWDPTGHI LMTCAKEENV KLWGPISGCW
RCLHSLCHPS TVNGIAWCSL PGKGSKLHLL MATGCQSGLV CVWRIPQDIT QTSVTSSEGW
WDQESSCQDG YRKSTGAKCV YQLRGHITPV RTVAFSSDGL ALVSGGLGGL MNIWSLRDGS
VLQTVVIGSG AIQTTVWIPD VGVAACSNRS KDVLVVNCTA EWAATNHVLA TCRTALKQQG
VLGLNMAPCM RAFLERLPVM LQEQYAYEKP HVVCGDQLVH SPYMQCLASL AVGLHLDQLL
CSPPVPPHHQ NCLPDPASWN PNEWAWLECF STTIKAAEAL TNGAQFPESF TVPDLEPVPE
DELIFLMDNS KWINGMDEQI MSWATSRPED WHLGGKCDVY LWGAGRHGQL AEAGRNVMVP
AAAPSFSQAQ QVICGQNCTF VIQANGTVLA CGEGSYGRLG QGNSDDLHVL TVISALQGFV
VTQLVTSCGS DGHSMALTES GEVFSWGDGD YGKLGHGNSD RQRRPRQIEA LQGEEVVQMS
CGFKHSAVVT SDGKLFTFGN GDYGRLGLGN TSNKKLPERV TALEGYQIGQ VACGLNHTLA
VSADGSMVWA FGDGDYGKLG LGNSTAKSSP QKVDVLCGIG IKKVACGTQF SVALTKDGHV
YTFGQDRLIG LPEGRARNHN RPQQIPVLAG VVIEDVAVGA EHTLALASTG DVYAWGSNSE
GQLGLGHTNH VREPTLVTVL QGKNVRQISA GRCHSAAWTA PPVPPRAPGV SVPLQLGLPD
AVPPQYGALR EVSIHTARAR LRLLYHFSDL MYSSWRLLNL SPNNQSSTSH YNAGTWGIVQ
GQLRPLLAPR VYTLPMVRSI GKTMVQGKNY GPQITVKRIS TRGRKCKPIF VQIARQVVKL
NASDLRLPSR AWKVKLVGEG ADDAGGVFDD TITEMCQELE TGIVDLLIPS PNATAEVGYN
RDRFLFNPSA CLDEHLMQFK FLGILMGVAI RTKKPLDLHL APVVWKQLCC VPLALEDLEE
VDLLYVQTLN SILHIEDSGI TEGSFHEMIP LDSFVGQSAD GKMVPIIPGG NSIPLTFSNR
KEYVERAIEY RLHEMDRQVA AVREGMSWIV PVPLLSLLTA KQLEQMVCGM PEISVDVLKK
VVRYREVDEL QQLVQWFWRT LEEFSNEERV LFMRFVSGRS RLPANTADIS QRFQIMKVDR
PYDSLPTSQT CFFQLRLPPY SSQLVMAERL RYAINNCRSI DMDNYMLSRN VDNAEGSDTD
Y
//
