ID A0A0Q3X2L2_AMAAE Unreviewed; 1860 AA.
AC A0A0Q3X2L2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit {ECO:0000256|ARBA:ARBA00015782};
DE EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
DE AltName: Full=O-GlcNAc transferase subunit p110 {ECO:0000256|ARBA:ARBA00029769};
DE AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit {ECO:0000256|ARBA:ARBA00031470};
GN ORFNames=AAES_183092 {ECO:0000313|EMBL:KQL56343.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL56343.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL56343.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL56343.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC transferase subfamily. {ECO:0000256|ARBA:ARBA00005386}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQL56343.1}.
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DR EMBL; LMAW01000436; KQL56343.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3X2L2; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.30.720.150; -; 1.
DR Gene3D; 3.40.50.11380; -; 2.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR006640; SprT-like_domain.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR44366; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF10263; SprT-like; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00731; SprT; 1.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 6.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1590..1610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1746..1770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1785..1805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1817..1838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 89..122
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 123..156
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 157..190
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 191..224
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 225..258
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 259..292
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 293..326
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 327..360
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 361..394
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 395..428
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 429..462
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1172..1336
FT /note="SprT-like"
FT /evidence="ECO:0000259|SMART:SM00731"
FT DOMAIN 1435..1538
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 1070..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1860 AA; 210449 MW; 6417A2A85F90377D CRC64;
MATSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA EXHCMQLWRQ EPDNTGVLLL
LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP
DFIDGYINLA AALVAAGDME GAVXAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY
LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI
FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
NALKEKGSVV EAEECYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF
AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR
AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT
DYDERMKKLV SIVADQLEKN RLPSVHPHHS MLYPLSHSFR KAIAERHGNL CLDKINVLHK
PSYEHPKDLK ASEGRLRIGY VSSDFGNHPT SHLMQSIPGM HNPDKFEIPC NGKAADRIHQ
DGIHILINMN GYTKGARNEL FALRPAPIQA MWLGYPGTSG ALFMDYIITD KETSPVEVAE
QYSEKLAYMP NTFFIGDHAN MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD
VKIVKMKCPD SCDNADGNAA LSMPVIPMNT IAEAVIEMIN RGQIQITING FNISNGLATT
QINNKAATGE EVPRTIIVTT RSQYGLPEDA VVYCNFNQLY KIDPSTLQMW ANILKRVPNS
VLWLLRFPAV GEPNIQQYAQ NLGLSQNRII FSPVAPKEEH VRRGQLADVC LDTPLCNGHT
TGMDVLWAGT PMVTMPGETL ASRVAASQLT CLGCLELIAK SRQEYEDIAV KLGTDLEYLK
KIRGKVWKQR ISSPLFNTKQ YTMDLERLYL QMWDHYAAGN KPDHMIKPVE ARQKDLQTMK
KWMPSGKKNS CCQELQYPEA SSDTDDSVFV ESDYQKGRVK DLKENXKRIK LPPPQNLRES
ISRGKNSKSP WVDGQPLKGK GVKTPRPNAX SLQETPSRIM APARTPGNKS VGRSQSAKTE
ERLRVCSVPG CFLQDLSNPR SHYVMYFKKN KEDLARKLYR LYNSTIFEQK LPDKMEIIWN
KKMRKTAGYC VTGLTEGPEA KRYARIELSE KVCDSADRLR DTLVHEACHA ATWLINGVRD
GHGRFWRYYA NKSSVIHPEL PIVARCHSYE INYKFIYECV LCKATRFVML NTLWWPKTTP
NPWFWVCKAG GNLRHFFGEK NVPFGISVAV LLPSCVQNSV LQVVVIGVAV RLARLVAALV
CMRSSRARLG EIQGRLLGCL PSSPXVPETP SSDVSSPFFW LQSCCNSTKM EGSKEKIILN
IGGVRYETYS STLQTFPGTK LCSLTEPNAS SIYDYDPTTK EFFFDRSAEI FSYVLNYYRT
KHFHCPIDTC RSVLEEELAF WEINEAQLAS CCWLKLNNRE VQPEEFDILD ENEQTEDQCL
IVQTERRDLS WRTRWQPKIW SMFEKPFSSF SAKCLAFVSL LFIVGIVIVF CEETKAQFEF
FTANFTSVGY SEVSHNDREP YYHQAAXLLH LELFCVLWFT FELSVRFCFC PDKKLFFKNP
LNVVDFLSLF PVYIELFVAG QIQRVPSLGL WLGFVRVIYL LKLLKISKLI ETPLILRVLC
YTLKSILREI CILLMILAFE TLFFGSLFFY GELLGSHPSY AGELHFTDIL VCFWWALITL
TTVGYGDIIP LTTAGQVTAA LAAVFGMLTI IIPIPIFLVK FKNYYDIAIF KQKLKRSXKL
//
