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Database: UniProt
Entry: H0UV09_CAVPO
LinkDB: H0UV09_CAVPO
Original site: H0UV09_CAVPO 
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
//
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