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Database: UniProt
Entry: A0A091HXD0_CALAN
LinkDB: A0A091HXD0_CALAN
Original site: A0A091HXD0_CALAN 
ID   A0A091HXD0_CALAN        Unreviewed;       557 AA.
AC   A0A091HXD0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
DE   Flags: Fragment;
GN   ORFNames=N300_14327 {ECO:0000313|EMBL:KFO99797.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO99797.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO99797.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO99797.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC         (1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC         dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC         Xref=Rhea:RHEA:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519,
CC         ChEBI:CHEBI:132520; EC=2.4.1.261;
CC         Evidence={ECO:0000256|ARBA:ARBA00034020};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-
CC         Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC         diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-
CC         D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29531,
CC         Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628,
CC         Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517;
CC         EC=2.4.1.259; Evidence={ECO:0000256|ARBA:ARBA00033991};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU363075}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC       {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
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DR   EMBL; KL217877; KFO99797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091HXD0; -.
DR   STRING; 9244.A0A091HXD0; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   PANTHER; PTHR22760:SF2; ALPHA-1,2-MANNOSYLTRANSFERASE ALG9; 1.
DR   PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363075,
KW   ECO:0000313|EMBL:KFO99797.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO99797.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363075};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363075}.
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        124..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        170..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        206..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        266..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        302..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        326..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   TRANSMEM        366..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363075"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO99797.1"
FT   NON_TER         557
FT                   /evidence="ECO:0000313|EMBL:KFO99797.1"
SQ   SEQUENCE   557 AA;  63806 MW;  9B11AAD6C62BADD9 CRC64;
     SGSKTGQVWA PEGSTAFKCL ISARFCAALL SNISDCDETF NYWEPTHYLV YGTGFQTWEY
     SPAYAIRSYA YLWLHALPAL FHARVLQTNK VLIFYFLRCF LAFLSCICEL YFYKAVCKKF
     GLHVGRLMLA FLVLSTGMFC SSAAFLPSSF CMYTTVVAMT GWYMDKTSVA VLGVAAGALL
     GWPFSAALGL PIAFDLLILK QRWKSFLNWC VVSLILFLVP LVVVDSYYYG KLVVAPLNIV
     LYNVFTPHGP DLYGTEPWTF YFINGFLNFN VAFILALLVL PLTCLMECLL QKFHVQNLGR
     PYWLTLSPMY IWIMIFFSQP HKEERFLFPI YPLICLCSAV ALSALQKCYH FIFQRYRLEH
     YTVSSNWLAL GTVFLFGLLS LSRSVALFRG YHGPLDLYPE FHRIATDPSI HTVPEGRAIN
     VCVGKEWHRF PSSFLLPDNW QLQFILSEFR GQLPKPFAKG ALATGIRMSV LLQIDISKCH
     YLVDLDTAAE SPREPRYSSN KEEWVTIAYK PFLDASRSSK LLRAFYIPFL SEQYTWYANY
     TILKPRRSKQ TRKKLGG
//
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