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Database: UniProt
Entry: H9G6I8_ANOCA
LinkDB: H9G6I8_ANOCA
Original site: H9G6I8_ANOCA 
ID   H9G6I8_ANOCA            Unreviewed;       634 AA.
AC   H9G6I8;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
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=galnt3 {ECO:0000313|Ensembl:ENSACAP00000002579.2};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002579.2, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000002579.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002579.2};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000002579.2}
RP   IDENTIFICATION.
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   RefSeq; XP_016854319.1; XM_016998830.1.
DR   RefSeq; XP_016854320.1; XM_016998831.1.
DR   RefSeq; XP_016854321.1; XM_016998832.1.
DR   AlphaFoldDB; H9G6I8; -.
DR   STRING; 28377.ENSACAP00000002579; -.
DR   Ensembl; ENSACAT00000002645.4; ENSACAP00000002579.2; ENSACAG00000002582.4.
DR   GeneID; 100557458; -.
DR   KEGG; acs:100557458; -.
DR   CTD; 2591; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000156609; -.
DR   InParanoid; H9G6I8; -.
DR   OMA; NPLFKMC; -.
DR   OrthoDB; 202750at2759; -.
DR   TreeFam; TF313267; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000002582; Expressed in dewlap and 11 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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:SF33; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 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, ECO:0000256|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361242};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361242}.
FT   TRANSMEM        21..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          507..631
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          110..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  72657 MW;  B7A191D7B8D2A227 CRC64;
     MAAYIKKLRR FVIKQLSQGK LWKFTFVIFI FLIFLVLLQR EVGIQDFNEE PGILSKDGKR
     SNVLGLVLKA VNNMKAVKPK MQIKAPIRQT QNAGPKRCLP GSYTTAELKS HLERPPQDSN
     APGASGKAFK TINLSPDEQK EKERGDEKHC FNAFASDRIS LHRDLGPDTR PPECIEQKFK
     RCPPLPTTSV IIVFHNEAWS TLLRTVHSVM YTSPAILLKE IILVDDASVD DYLQDKLDDY
     VKQFHIVKVV RQKERKGLIT ARLLGASIAT GETLTFLDAH CECFYGWLEP LLARIAENNT
     YVVSPDISSI DLNTFEFSKP SPYGQSHNRG NFDWSLSFGW ESLPEHESKK RKDETYPIKT
     PTFAGGLFSI SKDYFYNIGS YDEEMEIWGG ENIEMSFRVW QCGGQLEIIP CSVVGHVFRS
     KSPHSFPKGT QVITRNQVRL AEVWMDEYKN IFYRRNTEAA KIVKQQTFGD ISKRHELKQR
     LQCKDFKWYL SNVYPEAYVP DLNPPLSGFL KNVGRRACLD VGENNHGGKP LIMYTCHGLG
     GNQYFEYSAR HEIRHNIQKE LCLHASQGAV QLNECSYNGK KSRTSKEEKW EIREDQLLYN
     AELNMCLTGN WEHPSMVSCD PSDHFQKWIF GQNT
//
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