ALG9_HUMAN
ID ALG9_HUMAN Reviewed; 611 AA.
AC Q9H6U8; Q6ZMD5; Q7Z4R4; Q96GS7; Q96PB9; Q9H068;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Alpha-1,2-mannosyltransferase ALG9 {ECO:0000305};
DE EC=2.4.1.259 {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070};
DE EC=2.4.1.261 {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070};
DE AltName: Full=Asparagine-linked glycosylation protein 9 homolog {ECO:0000312|HGNC:HGNC:15672};
DE AltName: Full=Disrupted in bipolar disorder protein 1 {ECO:0000303|PubMed:12030331};
DE AltName: Full=Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000305};
DE AltName: Full=Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000305};
GN Name=ALG9 {ECO:0000312|HGNC:HGNC:15672};
GN Synonyms=DIBD1 {ECO:0000303|PubMed:12030331};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS ILE-289 AND LEU-506.
RX PubMed=12030331; DOI=10.1007/s10048-001-0129-x;
RA Baysal B.E., Willett-Brozick J.E., Badner J.A., Corona W., Ferrell R.E.,
RA Nimgaonkar V.L., Detera-Wadleigh S.D.;
RT "A mannosyltransferase gene at 11q23 is disrupted by a translocation
RT breakpoint that co-segregates with bipolar affective disorder in a small
RT family.";
RL Neurogenetics 4:43-53(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymphoma;
RA Guo J.H., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP ILE-289.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, VARIANT CDG1L
RP LYS-523, AND VARIANT ILE-289.
RX PubMed=15148656; DOI=10.1086/422367;
RA Frank C.G., Grubenmann C.E., Eyaid W., Berger E.G., Aebi M., Hennet T.;
RT "Identification and functional analysis of a defect in the human ALG9 gene:
RT definition of congenital disorder of glycosylation type IL.";
RL Am. J. Hum. Genet. 75:146-150(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND VARIANT CDG1L CYS-287.
RX PubMed=15945070; DOI=10.1002/ajmg.a.30851;
RA Weinstein M., Schollen E., Matthijs G., Neupert C., Hennet T.,
RA Grubenmann C.E., Frank C.G., Aebi M., Clarke J.T.R., Griffiths A.,
RA Seargeant L., Poplawski N.;
RT "CDG-IL: an infant with a novel mutation in the ALG9 gene and additional
RT phenotypic features.";
RL Am. J. Med. Genet. A 136:194-197(2005).
RN [8]
RP LACK OF ASSOCIATION WITH BIPOLAR AFFECTIVE DISORDERS.
RX PubMed=16859551; DOI=10.1186/1744-9081-2-25;
RA Baysal B.E., Willett-Brozick J.E., Bacanu S.A., Detera-Wadleigh S.,
RA Nimgaonkar V.L.;
RT "Common variations in ALG9 are not associated with bipolar I disorder: a
RT family-based study.";
RL Behav. Brain Funct. 2:25-25(2006).
RN [9]
RP INVOLVEMENT IN GIKANIS.
RX PubMed=25966638; DOI=10.1038/ejhg.2015.91;
RA Tham E., Eklund E.A., Hammarsjoe A., Bengtson P., Geiberger S.,
RA Lagerstedt-Robinson K., Malmgren H., Nilsson D., Grigelionis G., Conner P.,
RA Lindgren P., Lindstrand A., Wedell A., Albaage M., Zielinska K.,
RA Nordgren A., Papadogiannakis N., Nishimura G., Grigelioniene G.;
RT "A novel phenotype in N-glycosylation disorders: Gillessen-Kaesbach-
RT Nishimura skeletal dysplasia due to pathogenic variants in ALG9.";
RL Eur. J. Hum. Genet. 24:198-207(2016).
CC -!- FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid-
CC linked oligosaccharides. {ECO:0000269|PubMed:15148656,
CC ECO:0000269|PubMed:15945070}.
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:0000269|PubMed:15148656,
CC ECO:0000269|PubMed:15945070};
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:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15148656, ECO:0000269|PubMed:15945070}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:15148656}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H6U8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6U8-2; Sequence=VSP_015434;
CC Name=3;
CC IsoId=Q9H6U8-3; Sequence=VSP_015435;
CC Name=4;
CC IsoId=Q9H6U8-4; Sequence=VSP_015434, VSP_015435;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed; with highest levels in
CC heart, liver and pancreas. {ECO:0000269|PubMed:12030331}.
CC -!- DISEASE: Note=A chromosomal aberration involving ALG9 is found in a
CC family with bipolar affective disorder. Translocation t(9;11)(p24;q23).
CC However, common variations in ALG9 do not play a major role in
CC predisposition to bipolar affective disorder.
CC {ECO:0000269|PubMed:12030331}.
CC -!- DISEASE: Congenital disorder of glycosylation 1L (CDG1L) [MIM:608776]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:15148656,
CC ECO:0000269|PubMed:15945070}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Gillessen-Kaesbach-Nishimura syndrome (GIKANIS) [MIM:263210]:
CC A rare autosomal recessive syndrome characterized by severe skeletal
CC dysplasia, facial dysmorphic features, polycystic kidney disease and
CC other visceral malformations. It may be lethal in utero or early in
CC life. The skeletal features uniformly comprise a round pelvis,
CC mesomelic shortening of the upper limbs and defective ossification of
CC the cervical spine. {ECO:0000269|PubMed:25966638}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; AF395532; AAL25798.1; -; mRNA.
DR EMBL; AF454937; AAP97696.1; -; mRNA.
DR EMBL; AL136927; CAB66861.1; -; mRNA.
DR EMBL; AK025498; BAB15154.1; -; mRNA.
DR EMBL; AK172828; BAD18793.1; -; mRNA.
DR EMBL; BC009255; AAH09255.1; -; mRNA.
DR CCDS; CCDS41714.1; -. [Q9H6U8-4]
DR CCDS; CCDS53709.1; -. [Q9H6U8-2]
DR CCDS; CCDS73379.1; -. [Q9H6U8-1]
DR CCDS; CCDS73380.1; -. [Q9H6U8-3]
DR RefSeq; NP_001071158.1; NM_001077690.1. [Q9H6U8-1]
DR RefSeq; NP_001071159.1; NM_001077691.1. [Q9H6U8-4]
DR RefSeq; NP_001071160.1; NM_001077692.1. [Q9H6U8-2]
DR RefSeq; NP_079016.2; NM_024740.2. [Q9H6U8-3]
DR RefSeq; XP_016873808.1; XM_017018319.1.
DR RefSeq; XP_016873809.1; XM_017018320.1.
DR RefSeq; XP_016873810.1; XM_017018321.1.
DR RefSeq; XP_016873811.1; XM_017018322.1.
DR AlphaFoldDB; Q9H6U8; -.
DR BioGRID; 122893; 72.
DR IntAct; Q9H6U8; 32.
DR STRING; 9606.ENSP00000482396; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR GlyGen; Q9H6U8; 3 sites.
DR iPTMnet; Q9H6U8; -.
DR PhosphoSitePlus; Q9H6U8; -.
DR BioMuta; ALG9; -.
DR DMDM; 73921666; -.
DR EPD; Q9H6U8; -.
DR jPOST; Q9H6U8; -.
DR MassIVE; Q9H6U8; -.
DR MaxQB; Q9H6U8; -.
DR PaxDb; Q9H6U8; -.
DR PeptideAtlas; Q9H6U8; -.
DR PRIDE; Q9H6U8; -.
DR ProteomicsDB; 81040; -. [Q9H6U8-1]
DR ProteomicsDB; 81041; -. [Q9H6U8-2]
DR ProteomicsDB; 81042; -. [Q9H6U8-3]
DR ProteomicsDB; 81043; -. [Q9H6U8-4]
DR Antibodypedia; 51337; 73 antibodies from 14 providers.
DR DNASU; 79796; -.
DR Ensembl; ENST00000398006.6; ENSP00000381090.2; ENSG00000086848.15. [Q9H6U8-2]
DR Ensembl; ENST00000531154.5; ENSP00000435517.1; ENSG00000086848.15. [Q9H6U8-4]
DR Ensembl; ENST00000614444.4; ENSP00000484200.1; ENSG00000086848.15. [Q9H6U8-1]
DR Ensembl; ENST00000616540.5; ENSP00000482437.1; ENSG00000086848.15. [Q9H6U8-3]
DR GeneID; 79796; -.
DR KEGG; hsa:79796; -.
DR MANE-Select; ENST00000616540.5; ENSP00000482437.1; NM_024740.2; NP_079016.2. [Q9H6U8-3]
DR UCSC; uc001ply.4; human. [Q9H6U8-1]
DR CTD; 79796; -.
DR DisGeNET; 79796; -.
DR GeneCards; ALG9; -.
DR GeneReviews; ALG9; -.
DR HGNC; HGNC:15672; ALG9.
DR HPA; ENSG00000086848; Low tissue specificity.
DR MalaCards; ALG9; -.
DR MIM; 263210; phenotype.
DR MIM; 606941; gene.
DR MIM; 608776; phenotype.
DR neXtProt; NX_Q9H6U8; -.
DR OpenTargets; ENSG00000086848; -.
DR Orphanet; 79328; ALG9-CDG.
DR Orphanet; 730; Autosomal dominant polycystic kidney disease.
DR PharmGKB; PA134887582; -.
DR VEuPathDB; HostDB:ENSG00000086848; -.
DR eggNOG; KOG2515; Eukaryota.
DR eggNOG; KOG4174; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_018152_1_1_1; -.
DR InParanoid; Q9H6U8; -.
DR OMA; GKDWHRY; -.
DR OrthoDB; 1396421at2759; -.
DR PhylomeDB; Q9H6U8; -.
DR BRENDA; 2.4.1.259; 2681.
DR BRENDA; 2.4.1.261; 2681.
DR PathwayCommons; Q9H6U8; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR Reactome; R-HSA-4720454; Defective ALG9 causes CDG-1l.
DR SignaLink; Q9H6U8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79796; 67 hits in 1076 CRISPR screens.
DR ChiTaRS; ALG9; human.
DR GeneWiki; ALG9; -.
DR GenomeRNAi; 79796; -.
DR Pharos; Q9H6U8; Tbio.
DR PRO; PR:Q9H6U8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H6U8; protein.
DR Bgee; ENSG00000086848; Expressed in endothelial cell and 165 other tissues.
DR ExpressionAtlas; Q9H6U8; baseline and differential.
DR Genevisible; Q9H6U8; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039484; ALG9-like.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF2; PTHR22760:SF2; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement;
KW Congenital disorder of glycosylation; Disease variant;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..611
FT /note="Alpha-1,2-mannosyltransferase ALG9"
FT /id="PRO_0000215787"
FT TOPO_DOM 1..135
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..213
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..304
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..611
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 340
FT /note="Breakpoint for translocation"
FT /evidence="ECO:0000269|PubMed:12030331"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_015434"
FT VAR_SEQ 391
FT /note="Q -> QHSFLYFQ (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015435"
FT VARIANT 232
FT /note="A -> P (in dbSNP:rs36111204)"
FT /id="VAR_049221"
FT VARIANT 255
FT /note="S -> L (in dbSNP:rs17113312)"
FT /id="VAR_049222"
FT VARIANT 287
FT /note="Y -> C (in CDG1L; impairs activity;
FT dbSNP:rs121908023)"
FT /evidence="ECO:0000269|PubMed:15945070"
FT /id="VAR_023410"
FT VARIANT 289
FT /note="V -> I (in dbSNP:rs10502151)"
FT /evidence="ECO:0000269|PubMed:12030331,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15148656"
FT /id="VAR_023411"
FT VARIANT 506
FT /note="P -> L (in dbSNP:rs185149177)"
FT /evidence="ECO:0000269|PubMed:12030331"
FT /id="VAR_023412"
FT VARIANT 523
FT /note="E -> K (in CDG1L; impairs activity;
FT dbSNP:rs121908022)"
FT /evidence="ECO:0000269|PubMed:15148656"
FT /id="VAR_023413"
FT VARIANT 528
FT /note="I -> S (in dbSNP:rs12575909)"
FT /id="VAR_049223"
FT CONFLICT 309
FT /note="N -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 69863 MW; 51EC72DDBD866713 CRC64;
MASRGARQRL KGSGASSGDT APAADKLREL LGSREAGGAE HRTELSGNKA GQVWAPEGST
AFKCLLSARL CAALLSNISD CDETFNYWEP THYLIYGEGF QTWEYSPAYA IRSYAYLLLH
AWPAAFHARI LQTNKILVFY FLRCLLAFVS CICELYFYKA VCKKFGLHVS RMMLAFLVLS
TGMFCSSSAF LPSSFCMYTT LIAMTGWYMD KTSIAVLGVA AGAILGWPFS AALGLPIAFD
LLVMKHRWKS FFHWSLMALI LFLVPVVVID SYYYGKLVIA PLNIVLYNVF TPHGPDLYGT
EPWYFYLING FLNFNVAFAL ALLVLPLTSL MEYLLQRFHV QNLGHPYWLT LAPMYIWFII
FFIQPHKEER FLFPVYPLIC LCGAVALSAL QKCYHFVFQR YRLEHYTVTS NWLALGTVFL
FGLLSFSRSV ALFRGYHGPL DLYPEFYRIA TDPTIHTVPE GRPVNVCVGK EWYRFPSSFL
LPDNWQLQFI PSEFRGQLPK PFAEGPLATR IVPTDMNDQN LEEPSRYIDI SKCHYLVDLD
TMRETPREPK YSSNKEEWIS LAYRPFLDAS RSSKLLRAFY VPFLSDQYTV YVNYTILKPR
KAKQIRKKSG G
