ID H0UV09_CAVPO Unreviewed; 937 AA.
AC H0UV09;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644, ECO:0000256|RuleBase:RU361242};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361242};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
GN Name=GALNT5 {ECO:0000313|Ensembl:ENSCPOP00000000823.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000000823.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000000823.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000823.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU361242};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361242}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU361242}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU361242}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC ECO:0000256|RuleBase:RU361242}.
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DR EMBL; AAKN02005957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02005958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003478624.1; XM_003478576.2.
DR AlphaFoldDB; H0UV09; -.
DR STRING; 10141.ENSCPOP00000000823; -.
DR Ensembl; ENSCPOT00000000919.3; ENSCPOP00000000823.3; ENSCPOG00000000913.4.
DR GeneID; 100725254; -.
DR KEGG; cpoc:100725254; -.
DR CTD; 11227; -.
DR VEuPathDB; HostDB:ENSCPOG00000000913; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR InParanoid; H0UV09; -.
DR OMA; HGMHHVL; -.
DR OrthoDB; 202750at2759; -.
DR TreeFam; TF313267; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000913; Expressed in uterine cervix.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11675:SF130; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 5; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU361242};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361242};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU361242};
KW Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000256|RuleBase:RU361242};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 806..932
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 106498 MW; ABFFC7A8F97693EC CRC64;
MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NTRLLREDIV RREQIGFRVQ
ADQEKILSSS IRKMRPSPGG LGKRVWGKEN FRKIEDSVLE MGDDLDQAQK ERKMQNTLMK
GKVLPLWHPG HRQTPTGTLT KQKAEVKGSK SKAFSFQMTP RQTTVQGAQK SPFIAARRAA
LVNTSGYTET VSTKQEILKT HSLSSDTSKQ VAEGDITVTI DLRTNKTKQQ SQAVANKRTH
PANPPVPNSV EATASNKTET QNKELHAKKH KVHKGLPFFK LITDSKGLRK LSMNKTQLRG
LPEDVGTLKE QLNFSESHVV IITKEEELKT DTKKTSNSKI KTILPEIVDK SQGKQISRIR
SKASFPSPVL QKAIVSRTRN EIDEGLRPAG INLTAKAQPA EHKQSHAKVL VPEDHGMHQV
LKIDVTLSPR DPKAPGQFGR PVIVPPGKEK EAQKRWKEGN FNVYLSDLIP VDRAIEDTRP
AGCAEQLVHN QLPTTSIIMC FVDEVWSTLL RSVHSVLNRS PQHLIKEILL VDDFSTKDYL
KDKLDKYMSQ FPKVRILRLK ERHGLIRARL AGAQNATGDV LTFLDSHVEC NVGWLEPLLE
RVYLSRKKVA CPVIEVINDK DMSYMTVDNF QRGVFVWPMN FGWRTIPPEV VAKNRIKETD
VIRCPVMAGG LFSIDKNYFF ELGTYDPGLD VWGGENMELS FKVWMCGGEI EIVPCSRVGH
IFRNDNPYSF PKDRLKTVER NLVRVAEVWL DEYKELFYGH GDHLIDQRLD AGNLTQQREL
RKKLKCKSFK WYLDNVFPDL KAPIVRAGGV LVSVALSKCI SVENTTVILE ECDASSKSQQ
FNYTWLRLIK HEEWCLAPVP DKGALKLSTC DNRNSGLKWL HILTSVFHPD LVNHIVFENS
HQLLCLEGNF SQKTLKVAAC DSMKLHQKWK FEKYYED
//