SV2A_HUMAN
ID SV2A_HUMAN Reviewed; 742 AA.
AC Q7L0J3; D3DUZ7; O94841; Q5QNX8; Q7Z3L6; Q8NBJ6; Q9BVZ9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Synaptic vesicle glycoprotein 2A;
GN Name=SV2A; Synonyms=KIAA0736; ORFNames=PSEC0174;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Ovary;
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 [8]
RP CHARACTERIZATION AS BINDING-SITE FOR ANTIEPILEPTIC DRUG LEVETIRACETAM.
RX PubMed=15210974; DOI=10.1073/pnas.0308208101;
RA Lynch B.A., Lambeng N., Nocka K., Kensel-Hammes P., Bajjalieh S.M.,
RA Matagne A., Fuks B.;
RT "The synaptic vesicle protein SV2A is the binding site for the
RT antiepileptic drug levetiracetam.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9861-9866(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81 AND THR-84, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A2 RECEPTOR (MICROBIAL INFECTION),
RP AND SUBUNIT (MICROBIAL INFECTION).
RX PubMed=29649119; DOI=10.3390/toxins10040153;
RA Gustafsson R., Zhang S., Masuyer G., Dong M., Stenmark P.;
RT "Crystal structure of botulinum neurotoxin A2 in complex with the human
RT protein receptor SV2C reveals plasticity in receptor binding.";
RL Toxins 10:0-0(2018).
CC -!- FUNCTION: Plays a role in the control of regulated secretion in neural
CC and endocrine cells, enhancing selectively low-frequency
CC neurotransmission. Positively regulates vesicle fusion by maintaining
CC the readily releasable pool of secretory vesicles (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: (Microbial infection) Receptor for the C.botulinum neurotoxin
CC type A2 (BoNT/A, botA); glycosylation is not essential but enhances the
CC interaction (PubMed:29649119). Probably also serves as a receptor for
CC the closely related C.botulinum neurotoxin type A1.
CC {ECO:0000269|PubMed:29649119, ECO:0000305|PubMed:29649119}.
CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent
CC manner. Binds the adapter protein complex AP-2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is improved by
CC glycosylation of SV2 (PubMed:29649119). {ECO:0000305|PubMed:29649119}.
CC -!- SUBCELLULAR LOCATION: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules,
CC not present in adrenal microsomes. Associated with both insulin
CC granules and synaptic-like microvesicles in insulin-secreting cells of
CC the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor
CC synaptic terminals. {ECO:0000250|UniProtKB:Q02563,
CC ECO:0000250|UniProtKB:Q9JIS5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L0J3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L0J3-2; Sequence=VSP_019265;
CC -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
CC regulates interaction with SYT1. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Identified as the brain binding-site for the
CC antiepileptic drug levetiracetam/lev.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34456.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI12573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB018279; BAA34456.2; ALT_INIT; mRNA.
DR EMBL; AK075480; BAC11645.1; -; mRNA.
DR EMBL; BX537754; CAD97824.1; -; mRNA.
DR EMBL; AL591493; CAI12572.1; -; Genomic_DNA.
DR EMBL; AL591493; CAI12573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471121; EAW53596.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53598.1; -; Genomic_DNA.
DR EMBL; BC000776; AAH00776.2; -; mRNA.
DR EMBL; BC045111; AAH45111.1; -; mRNA.
DR CCDS; CCDS940.1; -. [Q7L0J3-1]
DR RefSeq; NP_001265648.1; NM_001278719.1.
DR RefSeq; NP_001315603.1; NM_001328674.1. [Q7L0J3-1]
DR RefSeq; NP_001315604.1; NM_001328675.1. [Q7L0J3-1]
DR RefSeq; NP_055664.3; NM_014849.4. [Q7L0J3-1]
DR PDB; 4V11; X-ray; 1.95 A; B=81-90.
DR PDBsum; 4V11; -.
DR AlphaFoldDB; Q7L0J3; -.
DR SMR; Q7L0J3; -.
DR BioGRID; 115229; 76.
DR IntAct; Q7L0J3; 13.
DR MINT; Q7L0J3; -.
DR STRING; 9606.ENSP00000358142; -.
DR ChEMBL; CHEMBL1998; -.
DR DrugBank; DB05541; Brivaracetam.
DR DrugBank; DB01202; Levetiracetam.
DR DrugBank; DB05885; Seletracetam.
DR DrugCentral; Q7L0J3; -.
DR GlyGen; Q7L0J3; 3 sites.
DR iPTMnet; Q7L0J3; -.
DR MetOSite; Q7L0J3; -.
DR PhosphoSitePlus; Q7L0J3; -.
DR BioMuta; SV2A; -.
DR DMDM; 74749878; -.
DR EPD; Q7L0J3; -.
DR jPOST; Q7L0J3; -.
DR MassIVE; Q7L0J3; -.
DR MaxQB; Q7L0J3; -.
DR PaxDb; Q7L0J3; -.
DR PeptideAtlas; Q7L0J3; -.
DR PRIDE; Q7L0J3; -.
DR ProteomicsDB; 68731; -. [Q7L0J3-1]
DR ProteomicsDB; 68732; -. [Q7L0J3-2]
DR Antibodypedia; 2184; 185 antibodies from 35 providers.
DR DNASU; 9900; -.
DR Ensembl; ENST00000369145.1; ENSP00000358141.1; ENSG00000159164.10. [Q7L0J3-2]
DR Ensembl; ENST00000369146.8; ENSP00000358142.3; ENSG00000159164.10. [Q7L0J3-1]
DR GeneID; 9900; -.
DR KEGG; hsa:9900; -.
DR MANE-Select; ENST00000369146.8; ENSP00000358142.3; NM_014849.5; NP_055664.3.
DR UCSC; uc001etg.4; human. [Q7L0J3-1]
DR CTD; 9900; -.
DR DisGeNET; 9900; -.
DR GeneCards; SV2A; -.
DR HGNC; HGNC:20566; SV2A.
DR HPA; ENSG00000159164; Tissue enhanced (brain, parathyroid gland).
DR MIM; 185860; gene.
DR neXtProt; NX_Q7L0J3; -.
DR OpenTargets; ENSG00000159164; -.
DR PharmGKB; PA128394564; -.
DR VEuPathDB; HostDB:ENSG00000159164; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q7L0J3; -.
DR OMA; FNDKSMV; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q7L0J3; -.
DR TreeFam; TF324824; -.
DR PathwayCommons; Q7L0J3; -.
DR Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (botD).
DR Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (botA).
DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (botF).
DR Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (botE).
DR SignaLink; Q7L0J3; -.
DR SIGNOR; Q7L0J3; -.
DR BioGRID-ORCS; 9900; 18 hits in 1071 CRISPR screens.
DR ChiTaRS; SV2A; human.
DR GeneWiki; SV2A; -.
DR GenomeRNAi; 9900; -.
DR Pharos; Q7L0J3; Tclin.
DR PRO; PR:Q7L0J3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7L0J3; protein.
DR Bgee; ENSG00000159164; Expressed in Brodmann (1909) area 10 and 152 other tissues.
DR Genevisible; Q7L0J3; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0014052; P:regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR022308; SV2.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasmic vesicle;
KW Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..742
FT /note="Synaptic vesicle glycoprotein 2A"
FT /id="PRO_0000239764"
FT TOPO_DOM 1..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..598
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with SYT1"
FT /evidence="ECO:0000250"
FT REGION 33..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02563"
FT MOD_RES 480
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 683..742
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_019265"
FT CONFLICT 100
FT /note="G -> D (in Ref. 4; CAD97824)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="D -> G (in Ref. 3; BAC11645)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="E -> G (in Ref. 4; CAD97824)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="V -> A (in Ref. 3; BAC11645)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="T -> A (in Ref. 3; BAC11645)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="G -> D (in Ref. 3; BAC11645)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="G -> R (in Ref. 3; BAC11645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 82695 MW; 913E216D5CFC2FB2 CRC64;
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEDDDDDFPA
PSDGYYRGEG TQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA
GVRGGLSDGE GPPGGRGEAQ RRKEREELAQ QYEAILRECG HGRFQWTLYF VLGLALMADG
VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS
VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF
FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW
GVRALSLGGQ VWGNFLSCFG PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY
ASRTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT
SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LINSTFLHNK EGCPLDVTGT GEGAYMVYFV
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVMSCVSCF FLSFGNSESA MIALLCLFGG
VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS
AALALGSSLA LKLPETRGQV LQ
