ALG14_CRYNJ
ID ALG14_CRYNJ Reviewed; 229 AA.
AC P0CM10; Q55XH5; Q5KMF9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14;
DE AltName: Full=Asparagine-linked glycosylation protein 14;
GN Name=ALG14; OrderedLocusNames=CNB01840;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Involved in protein N-glycosylation. Essential for the second
CC step of the dolichol-linked oligosaccharide pathway. Anchors the
CC catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with ALG13 to form a functional enzyme.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ALG14 family. {ECO:0000305}.
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DR EMBL; AE017342; AAW41698.1; -; Genomic_DNA.
DR RefSeq; XP_569005.1; XM_569005.1.
DR AlphaFoldDB; P0CM10; -.
DR STRING; 5207.AAW41698; -.
DR PaxDb; P0CM10; -.
DR eggNOG; KOG3339; Eukaryota.
DR HOGENOM; CLU_064541_0_1_1; -.
DR InParanoid; P0CM10; -.
DR OMA; GPGTCCI; -.
DR OrthoDB; 1449763at2759; -.
DR Proteomes; UP000002149; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IBA:GO_Central.
DR InterPro; IPR013969; Oligosacch_biosynth_Alg14.
DR PANTHER; PTHR12154; PTHR12154; 1.
DR Pfam; PF08660; Alg14; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..229
FT /note="UDP-N-acetylglucosamine transferase subunit ALG14"
FT /id="PRO_0000123813"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P38242"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38242"
SQ SEQUENCE 229 AA; 25806 MW; D11CB3899C551782 CRC64;
MSLGRYIGWS ILAFTYLVLA ILLRLIFLQP SKTSRASYRP KDAKCSLGVF LGSGGHTSEM
KALLSTLDYE RYQPRTYIYC HGDDLSLRAV SDIESSKGGL ISSKMYYLLS LPRARRVGQP
LLSTMVSVLK TLYIAALRLF LIPLLKNPRR PFVDLLIVNG PGTCVVLVLV SYIRRVRLEY
TRIIYVESFA RVKSLSLSGK MIRPLADRFL VQWPDASDSD NVIHKGLLV