ID VACHT_HUMAN Reviewed; 532 AA. AC Q16572; B2R7S1; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Vesicular acetylcholine transporter; DE Short=VAChT; DE AltName: Full=Solute carrier family 18 member 3; GN Name=SLC18A3; Synonyms=VACHT; 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 [GENOMIC DNA / MRNA], AND VARIANT GLU-520. RC TISSUE=Brain; RX PubMed=8071310; DOI=10.1016/s0021-9258(17)31734-9; RA Erickson J.D., Varoqui H., Schafer M.K.-H., Modi W., Diebler M.-F., RA Weihe E., Rand J.B., Eiden L.E., Bonner T.I., Usdin T.B.; RT "Functional identification of a vesicular acetylcholine transporter and its RT expression from a 'cholinergic' gene locus."; RL J. Biol. Chem. 269:21929-21932(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-520. RC TISSUE=Thalamus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-520. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-520. RC TISSUE=Brain; 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, TRANSPORT ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=8910293; DOI=10.1074/jbc.271.44.27229; RA Varoqui H., Erickson J.D.; RT "Active transport of acetylcholine by the human vesicular acetylcholine RT transporter."; RL J. Biol. Chem. 271:27229-27232(1996). RN [7] RP INTERACTION WITH SEC14L1. RX PubMed=17092608; DOI=10.1016/j.neuint.2006.09.010; RA Ribeiro F.M., Ferreira L.T., Marion S., Fontes S., Gomez M., Ferguson S.S., RA Prado M.A., Prado V.F.; RT "SEC14-like protein 1 interacts with cholinergic transporters."; RL Neurochem. Int. 50:356-364(2007). RN [8] RP FUNCTION, TRANSPORT ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF RP GLU-309 AND ASP-398, AND SITE. RX PubMed=20225888; DOI=10.1021/bi901953j; RA Khare P., Ojeda A.M., Chandrasekaran A., Parsons S.M.; RT "Possible important pair of acidic residues in vesicular acetylcholine RT transporter."; RL Biochemistry 49:3049-3059(2010). RN [9] RP FUNCTION, TRANSPORT ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=25355561; DOI=10.1038/srep06836; RA Hiasa M., Miyaji T., Haruna Y., Takeuchi T., Harada Y., Moriyama S., RA Yamamoto A., Omote H., Moriyama Y.; RT "Identification of a mammalian vesicular polyamine transporter."; RL Sci. Rep. 4:6836-6836(2014). RN [10] RP VARIANTS CMS21 ALA-186 AND HIS-398, AND INVOLVEMENT IN CMS21. RX PubMed=27590285; DOI=10.1212/wnl.0000000000003179; RA O'Grady G.L., Verschuuren C., Yuen M., Webster R., Menezes M., Fock J.M., RA Pride N., Best H.A., Benavides Damm T., Turner C., Lek M., Engel A.G., RA North K.N., Clarke N.F., MacArthur D.G., Kamsteeg E.J., Cooper S.T.; RT "Variants in SLC18A3, vesicular acetylcholine transporter, cause congenital RT myasthenic syndrome."; RL Neurology 87:1442-1448(2016). CC -!- FUNCTION: Electrogenic antiporter that exchanges one cholinergic CC neurotransmitter, acetylcholine or choline, with two intravesicular CC protons across the membrane of synaptic vesicles. Uses the CC electrochemical proton gradient established by the V-type proton-pump CC ATPase to store neurotransmitters inside the vesicles prior to their CC release via exocytosis (PubMed:8910293, PubMed:20225888) (By CC similarity). Determines cholinergic vesicular quantal size at CC presynaptic nerve terminals in developing neuro-muscular junctions with CC an impact on motor neuron differentiation and innervation pattern (By CC similarity). Part of forebrain cholinergic system, regulates CC hippocampal synapse transmissions that underlie spatial memory CC formation (By similarity). Can transport serotonin. CC {ECO:0000250|UniProtKB:O35304, ECO:0000250|UniProtKB:Q62666, CC ECO:0000269|PubMed:20225888, ECO:0000269|PubMed:25355561, CC ECO:0000269|PubMed:8910293}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetylcholine(out) + 2 H(+)(in) = acetylcholine(in) + 2 CC H(+)(out); Xref=Rhea:RHEA:72891, ChEBI:CHEBI:15355, CC ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:20225888, CC ECO:0000269|PubMed:25355561, ECO:0000269|PubMed:8910293}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72892; CC Evidence={ECO:0000305|PubMed:8910293}; CC -!- CATALYTIC ACTIVITY: CC Reaction=choline(in) + 2 H(+)(out) = choline(out) + 2 H(+)(in); CC Xref=Rhea:RHEA:73819, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; CC Evidence={ECO:0000250|UniProtKB:Q62666}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73820; CC Evidence={ECO:0000250|UniProtKB:Q62666}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out); CC Xref=Rhea:RHEA:73743, ChEBI:CHEBI:15378, ChEBI:CHEBI:350546; CC Evidence={ECO:0000269|PubMed:25355561}; CC -!- ACTIVITY REGULATION: Potently inhibited by L-vesamicol, reserpine and CC tetrabenazine. {ECO:0000269|PubMed:25355561, CC ECO:0000269|PubMed:8910293}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.97 mM for acetylcholine {ECO:0000269|PubMed:8910293}; CC KM=0.75 mM for acetylcholine {ECO:0000269|PubMed:20225888}; CC Vmax=0.58 nmol/min/mg enzyme toward acetylcholine CC {ECO:0000269|PubMed:8910293}; CC pH dependence: CC Optimum pH is 7. {ECO:0000269|PubMed:20225888}; CC -!- SUBUNIT: Interacts with SEC14L1. {ECO:0000269|PubMed:17092608}. CC -!- INTERACTION: CC Q16572; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-17598000, EBI-9083477; CC Q16572; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-17598000, EBI-11956541; CC Q16572; I3L0A0: PEDS1-UBE2V1; NbExp=3; IntAct=EBI-17598000, EBI-12213001; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic CC vesicle membrane {ECO:0000250|UniProtKB:Q62666}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Peripheral and central cholinergic nervous systems. CC {ECO:0000269|PubMed:8071310}. CC -!- DISEASE: Myasthenic syndrome, congenital, 21, presynaptic (CMS21) CC [MIM:617239]: A form of congenital myasthenic syndrome, a group of CC disorders characterized by failure of neuromuscular transmission, CC including pre-synaptic, synaptic, and post-synaptic disorders that are CC not of autoimmune origin. Clinical features are easy fatigability and CC muscle weakness. CMS21 is an autosomal recessive, pre-synaptic form CC characterized by ptosis, ophthalmoplegia, fatigable weakness, apneic CC crises, and deterioration of symptoms in cold water. Learning CC difficulties and left ventricular dysfunction may be present in some CC patients. {ECO:0000269|PubMed:27590285}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular CC transporter family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10554; AAB92675.1; -; Genomic_DNA. DR EMBL; U09210; AAA20497.1; -; mRNA. DR EMBL; AK313094; BAG35918.1; -; mRNA. DR EMBL; AC073366; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471187; EAW93093.1; -; Genomic_DNA. DR EMBL; BC007765; AAH07765.1; -; mRNA. DR CCDS; CCDS7231.1; -. DR PIR; I38658; I38658. DR RefSeq; NP_003046.2; NM_003055.2. DR AlphaFoldDB; Q16572; -. DR SMR; Q16572; -. DR BioGRID; 112460; 7. DR IntAct; Q16572; 4. DR STRING; 9606.ENSP00000363229; -. DR BindingDB; Q16572; -. DR ChEMBL; CHEMBL4767; -. DR GuidetoPHARMACOLOGY; 1013; -. DR TCDB; 2.A.1.2.28; the major facilitator superfamily (mfs). DR GlyCosmos; Q16572; 2 sites, No reported glycans. DR GlyGen; Q16572; 2 sites. DR iPTMnet; Q16572; -. DR PhosphoSitePlus; Q16572; -. DR BioMuta; SLC18A3; -. DR DMDM; 313104043; -. DR jPOST; Q16572; -. DR MassIVE; Q16572; -. DR PaxDb; 9606-ENSP00000363229; -. DR PeptideAtlas; Q16572; -. DR ProteomicsDB; 60925; -. DR ABCD; Q16572; 1 sequenced antibody. DR Antibodypedia; 27651; 302 antibodies from 23 providers. DR DNASU; 6572; -. DR Ensembl; ENST00000374115.5; ENSP00000363229.3; ENSG00000187714.7. DR GeneID; 6572; -. DR KEGG; hsa:6572; -. DR MANE-Select; ENST00000374115.5; ENSP00000363229.3; NM_003055.3; NP_003046.2. DR UCSC; uc001jhw.3; human. DR AGR; HGNC:10936; -. DR CTD; 6572; -. DR DisGeNET; 6572; -. DR GeneCards; SLC18A3; -. DR HGNC; HGNC:10936; SLC18A3. DR HPA; ENSG00000187714; Tissue enriched (brain). DR MalaCards; SLC18A3; -. DR MIM; 600336; gene. DR MIM; 617239; phenotype. DR neXtProt; NX_Q16572; -. DR OpenTargets; ENSG00000187714; -. DR Orphanet; 994; Fetal akinesia deformation sequence. DR Orphanet; 98914; Presynaptic congenital myasthenic syndromes. DR PharmGKB; PA326; -. DR VEuPathDB; HostDB:ENSG00000187714; -. DR eggNOG; KOG3764; Eukaryota. DR GeneTree; ENSGT00940000159449; -. DR HOGENOM; CLU_001265_10_9_1; -. DR InParanoid; Q16572; -. DR OMA; TRTPEVW; -. DR OrthoDB; 1429709at2759; -. DR PhylomeDB; Q16572; -. DR TreeFam; TF313494; -. DR PathwayCommons; Q16572; -. DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; Q16572; -. DR BioGRID-ORCS; 6572; 15 hits in 1138 CRISPR screens. DR GenomeRNAi; 6572; -. DR Pharos; Q16572; Tchem. DR PRO; PR:Q16572; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q16572; Protein. DR Bgee; ENSG00000187714; Expressed in primordial germ cell in gonad and 39 other cell types or tissues. DR GO; GO:0030121; C:AP-1 adaptor complex; IBA:GO_Central. DR GO; GO:0030122; C:AP-2 adaptor complex; IBA:GO_Central. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0060201; C:clathrin-sculpted acetylcholine transport vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central. DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005278; F:acetylcholine:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0015311; F:monoamine:proton antiporter activity; IDA:UniProtKB. DR GO; GO:0051630; P:acetylcholine uptake; IDA:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome. DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; ISS:UniProtKB. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB. DR GO; GO:1904398; P:positive regulation of neuromuscular junction development; ISS:UniProtKB. DR GO; GO:0051610; P:serotonin uptake; IDA:UniProtKB. DR CDD; cd17383; MFS_SLC18A3_VAChT; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR23506; -; 1. DR PANTHER; PTHR23506:SF13; VESICULAR ACETYLCHOLINE TRANSPORTER; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. DR Genevisible; Q16572; HS. PE 1: Evidence at protein level; KW Congenital myasthenic syndrome; Cytoplasmic vesicle; Disease variant; KW Glycoprotein; Membrane; Neurotransmitter transport; Reference proteome; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..532 FT /note="Vesicular acetylcholine transporter" FT /id="PRO_0000127517" FT TOPO_DOM 1..33 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 34..54 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 55..125 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 147..152 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 153..173 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 174..182 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 183..203 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 204..213 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 214..234 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 235..242 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 264..289 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 311..325 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 326..346 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 347..356 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 357..377 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 378..388 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 389..409 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 410..422 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 423..443 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 444..447 FT /note="Lumenal, vesicle" FT /evidence="ECO:0000255" FT TRANSMEM 448..468 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 469..532 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 471..532 FT /note="Mediates interaction with SEC14L1" FT /evidence="ECO:0000250|UniProtKB:O35304" FT REGION 502..523 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 193 FT /note="Important for transporter activity" FT /evidence="ECO:0000250|UniProtKB:Q62666" FT SITE 398 FT /note="Important for transporter activity" FT /evidence="ECO:0000269|PubMed:20225888" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 96 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 11 FT /note="R -> Q (in dbSNP:rs8187732)" FT /id="VAR_029152" FT VARIANT 13 FT /note="A -> P (in dbSNP:rs8187733)" FT /id="VAR_020034" FT VARIANT 29 FT /note="R -> W (in dbSNP:rs8187734)" FT /id="VAR_020035" FT VARIANT 186 FT /note="G -> A (in CMS21; dbSNP:rs1057517665)" FT /evidence="ECO:0000269|PubMed:27590285" FT /id="VAR_078030" FT VARIANT 398 FT /note="D -> H (in CMS21; dbSNP:rs1057517666)" FT /evidence="ECO:0000269|PubMed:27590285" FT /id="VAR_078031" FT VARIANT 520 FT /note="A -> E (in dbSNP:rs8187730)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8071310, FT ECO:0000269|Ref.4" FT /id="VAR_024638" FT MUTAGEN 309 FT /note="E->A,K: Loss of activity." FT /evidence="ECO:0000269|PubMed:20225888" FT MUTAGEN 309 FT /note="E->D: Has normal transporter activity. Retains the FT transporter activity; when associated with E-398." FT /evidence="ECO:0000269|PubMed:20225888" FT MUTAGEN 309 FT /note="E->Q: Has normal transporter activity. Loss of FT activity; when associated with N-398." FT /evidence="ECO:0000269|PubMed:20225888" FT MUTAGEN 398 FT /note="D->N: Loss of activity." FT /evidence="ECO:0000269|PubMed:20225888" SQ SEQUENCE 532 AA; 56903 MW; 445CDF48F08ED31D CRC64; MESAEPAGQA RAAATKLSEA VGAALQEPRR QRRLVLVIVC VALLLDNMLY MVIVPIVPDY IAHMRGGGEG PTRTPEVWEP TLPLPTPANA SAYTANTSAS PTAAWPAGSA LRPRYPTESE DVKIGVLFAS KAILQLLVNP LSGPFIDRMS YDVPLLIGLG VMFASTVLFA FAEDYATLFA ARSLQGLGSA FADTSGIAMI ADKYPEEPER SRALGVALAF ISFGSLVAPP FGGILYEFAG KRVPFLVLAA VSLFDALLLL AVAKPFSAAA RARANLPVGT PIHRLMLDPY IAVVAGALTT CNIPLAFLEP TIATWMKHTM AASEWEMGMA WLPAFVPHVL GVYLTVRLAA RYPHLQWLYG ALGLAVIGAS SCIVPACRSF APLVVSLCGL CFGIALVDTA LLPTLAFLVD VRHVSVYGSV YAIADISYSV AYALGPIVAG HIVHSLGFEQ LSLGMGLANL LYAPVLLLLR NVGLLTRSRS ERDVLLDEPP QGLYDAVRLR ERPVSGQDGE PRSPPGPFDA CEDDYNYYYT RS //