ID A0A2D0RFB3_ICTPU Unreviewed; 1052 AA.
AC A0A2D0RFB3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=ogt.1 {ECO:0000313|RefSeq:XP_017329229.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017329229.1};
RN [1] {ECO:0000313|RefSeq:XP_017329229.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017329229.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_017329229.1; XM_017473740.3.
DR AlphaFoldDB; A0A2D0RFB3; -.
DR STRING; 7998.ENSIPUP00000024696; -.
DR Ensembl; ENSIPUT00000025728; ENSIPUP00000024696; ENSIPUG00000016652.
DR GeneID; 108268666; -.
DR CTD; 337685; -.
DR OrthoDB; 34780at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000221080; Chromosome 8.
DR GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.720.150; -; 1.
DR Gene3D; 3.40.50.11380; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
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; PF13844; Glyco_transf_41; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 12.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 5.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_017329229.1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|RefSeq:XP_017329229.1}.
FT REPEAT 79..112
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 113..146
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 147..180
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 181..214
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 215..248
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 249..282
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 283..316
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 317..350
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 351..384
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 385..418
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 419..452
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 466..1020
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1052 AA; 117130 MW; 781D0915A1422981 CRC64;
MASSVGNVAD STGLAELAHR EYQSGDFEAA ERHCMQLWRQ EPDNTGVLLL LSSIHFQCRR
LDRSAHFSTL AIKQNPMLAE AYSNLGNVFK ERGQLQEAIE HYRHALRLKP DFIDGYINLA
AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF
AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAGYLR
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGNVS
EAEECYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVQLY RKALEVFPEF AAAHSNLASV
LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR AIQINPAFAD
AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV
SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINALHK PAYEHPKDLK
ASGGRLRVGY VSSDFGNHPT SHLMQSIPGM HNSEKFEVFC YALSPDDSTN FRVKVIAEAH
HFTDLSQITC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA MWLGYPGTSG
APFMDYIITD KETSPVEVAE QYSEKMAYMP NTFFIGDHAN MFPHLKKKAV IDFKSNGHIF
DNRIVLNGID LKAFLDSLPD VKVIKMECDS QESTDNNGAL SMPVIPMNTA AEAIINMINQ
GQIQVTINSF TVSNGLATTQ IFTVEEVVVS GTVALQINNK AATGEEVPRT IVVTTRSQYG
LPEDSIVYCN FNQLYKIDPP TLQMWANILK RVPNSVLWLL RFPAVGEPNI QQYAQSMGLA
ASRIIFSPVA PKEEHVRRGQ LADVCLDTPL CNGHTTGMDV LWAGTPMVTM PGETLASRVA
ASQLTCLGCP ELIAQSRQEY EDVAVKLGTD MDYLKKIRSR VWKQRICSPL FNTKQYTVDL
ERLYLQMWEH HASGGKPDHL VKMQLLDSSE SA
//
