ID A0A1S3SWC6_SALSA Unreviewed; 1038 AA.
AC A0A1S3SWC6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LOC100380730 {ECO:0000313|RefSeq:XP_014068640.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014068640.1};
RN [1] {ECO:0000313|RefSeq:XP_014068640.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014068640.1};
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_014068640.1; XM_014213165.1.
DR AlphaFoldDB; A0A1S3SWC6; -.
DR GeneID; 100380730; -.
DR OrthoDB; 34780at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR Bgee; ENSSSAG00000061261; Expressed in brain and 15 other cell types or tissues.
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_014068640.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW 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_014068640.1}.
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..1006
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
SQ SEQUENCE 1038 AA; 115605 MW; AE67047AA09A8BED CRC64;
MASSVGNVAD STGLAELAHR EYQSGDFEAA ERHCMQLWRQ EPDNTGVLLL LSSIHFQCRR
LDRSAHFSTL AIKQNSMLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP DFIDGYINLA
AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF
AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAGYLR
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGNVS
EAEECYNTAL RLCPTHADSL NNLANIKREQ GNIEDAVQLY RKALEVFPEF AAAHSNLASV
LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR AIQINPAFAD
AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV
SIVADQLDKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINALHK PAFEYPKDLK
ASAGRLRVGY VSSDFGNHPT SHLMQSIPGM HNSDKFEVFC YALSPDDNTN FRVKVVAEAH
HFTDLSQLPC NGKAADRIHQ DGLHILVNMN GYTKGARNEL FALRPAPIQC MWLGYPGTSG
APFMDYIVSD KETSPFEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV IDFKSNGHIF
DNRIVLNGID LKAFLDSLPD VKVVKMKCSI GESGAAETNG ALSMPVIPMN TAAEAIINMI
NQGQIQVTIN GFTVSNGLAT TQLNNKAATG EEVPRTIVVT TRSQYGLPED SIVYCNFNQL
YKIDPPTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNFGLPGSRI IFSPVAPKEE
HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL QCLGCPELIA
HTRQEYEDVA VKLGCDMEYL KMIRSRVWKQ RICSPLFNTK QYTMDLEKLY LQMWERHASG
GKPDHLVKLQ PVESSESA
//
