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Database: UniProt
Entry: H0V1B1_CAVPO
LinkDB: H0V1B1_CAVPO
Original site: H0V1B1_CAVPO 
ID   H0V1B1_CAVPO            Unreviewed;       567 AA.
AC   H0V1B1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   24-JAN-2024, entry version 75.
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=GALNT2 {ECO:0000313|Ensembl:ENSCPOP00000003271.3};
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:ENSCPOP00000003271.3, 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:ENSCPOP00000003271.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003271.3};
RG   Ensembl;
RL   Submitted (JUL-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; AAKN02021623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003473535.2; XM_003473487.3.
DR   AlphaFoldDB; H0V1B1; -.
DR   STRING; 10141.ENSCPOP00000003271; -.
DR   Ensembl; ENSCPOT00000003667.3; ENSCPOP00000003271.3; ENSCPOG00000003623.4.
DR   GeneID; 100724116; -.
DR   KEGG; cpoc:100724116; -.
DR   CTD; 2590; -.
DR   VEuPathDB; HostDB:ENSCPOG00000003623; -.
DR   eggNOG; KOG3738; Eukaryota.
DR   GeneTree; ENSGT00940000156958; -.
DR   HOGENOM; CLU_013477_0_2_1; -.
DR   InParanoid; H0V1B1; -.
DR   OMA; QEWAFSK; -.
DR   OrthoDB; 202750at2759; -.
DR   TreeFam; TF313267; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000003623; Expressed in uterine cervix and 13 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016266; P:O-glycan processing; IEA:Ensembl.
DR   GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR   GO; GO:0018242; P:protein O-linked glycosylation via serine; IEA:Ensembl.
DR   GO; GO:0018243; P:protein O-linked glycosylation via threonine; IEA:Ensembl.
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:SF49; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 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 {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..567
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011688800"
FT   DOMAIN          437..562
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          48..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   567 AA;  64474 MW;  15D5D4A8A409E0F1 CRC64;
     MRRRSRVLLC FALLWVLGIA YYMYSGGGSA LAAGGSRKED WNEIDPIKKK DLHHSNGDEK
     AQSMETLPPG KVRWPDFNQE AYVGGTMVRS GQDPYARNKF NQVESDKLRM DRAIPDTRHE
     QCQRKQWRVD LPATSVVITF HNEARSALLR TVVSVLKRSP PHLIKEIILV DDYSNDPEDG
     ALLGKIEKVR VLRNDRREGL MRSRVRGADA AQAKVLTFLD SHCECNEHWL EPLLERVAED
     RTRVVSPIID VINMDNFQYV GASADLKGGF DWNLVFKWDY MTPEQRRSRQ GNPVAPIKTP
     MIAGGLFVMD KLYFEELGKY DMMMDVWGGE NLEISFRVWQ CGGSLEIIPC SRVGHVFRKQ
     HPYTFPGGSG TVFARNTRRA AEVWMDEYKN FYYAAVPSAR NVPYGNIQSR LELRKRLGCR
     PFQWYLENVY PELRVPDHQD IAFGALQQGT NCLDTLGHFA DGVVGIYECH NAGGNQEWAL
     TKEKSVKHMD LCLTVVDRAP GALVKLQGCR ENDSRQKWEQ IESNSKLRHV GSNLCLDSRT
     AKSGGLSVEV CGPALSQQWK FSLNLQQ
//
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