VGLU1_HUMAN
ID VGLU1_HUMAN Reviewed; 560 AA.
AC Q9P2U7; B4DFR9; B4DG46; Q6PCD0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vesicular glutamate transporter 1 {ECO:0000250|UniProtKB:Q3TXX4};
DE Short=VGluT1 {ECO:0000250|UniProtKB:Q3TXX4};
DE AltName: Full=Brain-specific Na(+)-dependent inorganic phosphate cotransporter {ECO:0000303|PubMed:10820226};
DE AltName: Full=Solute carrier family 17 member 7;
GN Name=SLC17A7 {ECO:0000312|HGNC:HGNC:16704};
GN Synonyms=BNPI {ECO:0000303|PubMed:10820226}, VGLUT1;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10820226; DOI=10.1046/j.1471-4159.2000.0742622.x;
RA Aihara Y., Mashima H., Onda H., Hisano S., Kasuya H., Hori T., Yamada S.,
RA Tomura H., Yamada Y., Inoue I., Kojima I., Takeda J.;
RT "Molecular cloning of a novel brain-type Na(+)-dependent inorganic
RT phosphate cotransporter.";
RL J. Neurochem. 74:2622-2625(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Amygdala;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-431.
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).
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, proton, potassium, sodium and
CC phosphate (PubMed:10820226). At the synaptic vesicle membrane, mainly
CC functions as an uniporter which transports preferentially L-glutamate
CC but also phosphate from the cytoplasm into synaptic vesicles at
CC presynaptic nerve terminals of excitatory neural cells (By similarity).
CC The L-glutamate or phosphate uniporter activity is electrogenic and is
CC driven by the proton electrochemical gradient, mainly by the electrical
CC gradient established by the vacuolar H(+)-ATPase across the synaptic
CC vesicle membrane (By similarity). In addition, functions as a chloride
CC channel that allows a chloride permeation through the synaptic vesicle
CC membrane that affects the proton electrochemical gradient and promotes
CC synaptic vesicles acidification (By similarity). Moreover, may function
CC as a K(+)/H(+) antiport allowing to maintain the electrical gradient
CC and to decrease chemical gradient and therefore sustain vesicular
CC glutamate uptake (By similarity). The vesicular K(+)/H(+) antiport
CC activity is electroneutral (By similarity). At the plasma membrane,
CC following exocytosis, functions as a symporter of Na(+) and phosphate
CC from the extracellular space to the cytoplasm allowing synaptic
CC phosphate homeostasis regulation (PubMed:10820226). The symporter
CC activity is driven by an inside negative membrane potential and is
CC electrogenic (By similarity). Is necessary for synaptic signaling of
CC visual-evoked responses from photoreceptors (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634,
CC ECO:0000269|PubMed:10820226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q62634};
CC -!- ACTIVITY REGULATION: Chloride channel activity is allosterically
CC activated by lumenal H(+) and Cl(-) leading to synaptic vesicles
CC acidification. The L-glutamate transport activity is allosterically
CC activated by lumenal H(+) and Cl(-). The allosteric activation by H(+)
CC efficiently prevents non-vesicular efflux across the plasma membrane,
CC thereby restricting L-glutamate transport activity to acidic membranes
CC such as synaptic vesicles. {ECO:0000250|UniProtKB:Q62634}.
CC -!- SUBUNIT: Interacts with SHANK3. {ECO:0000250|UniProtKB:Q3TXX4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q3TXX4}. Cell membrane
CC {ECO:0000305|PubMed:10820226}; Multi-pass membrane protein
CC {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q3TXX4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2U7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2U7-2; Sequence=VSP_056110;
CC Name=3;
CC IsoId=Q9P2U7-3; Sequence=VSP_056111;
CC -!- TISSUE SPECIFICITY: Expressed in several regions of the brain including
CC amygdala, cerebellum, cerebral cortex, hippocampus, frontal lobe,
CC medulla, occipital lobe, putamen and temporal lobe.
CC {ECO:0000269|PubMed:10820226}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
CC -!- CAUTION: Martineau M. et al. show that may function as a L-
CC glutamate/H(+) antiporter (By similarity). However, according to
CC Eriksen J. et al., H(+) is an allosteric activator (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX4, ECO:0000250|UniProtKB:Q62634}.
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DR EMBL; AB032436; BAA92875.1; -; mRNA.
DR EMBL; AK294226; BAG57530.1; -; mRNA.
DR EMBL; AK294405; BAG57657.1; -; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52485.1; -; Genomic_DNA.
DR EMBL; BC059379; AAH59379.1; -; mRNA.
DR CCDS; CCDS12764.1; -. [Q9P2U7-1]
DR RefSeq; NP_064705.1; NM_020309.3. [Q9P2U7-1]
DR AlphaFoldDB; Q9P2U7; -.
DR SMR; Q9P2U7; -.
DR BioGRID; 121331; 1.
DR IntAct; Q9P2U7; 2.
DR STRING; 9606.ENSP00000221485; -.
DR TCDB; 2.A.1.14.30; the major facilitator superfamily (mfs).
DR iPTMnet; Q9P2U7; -.
DR PhosphoSitePlus; Q9P2U7; -.
DR SwissPalm; Q9P2U7; -.
DR BioMuta; SLC17A7; -.
DR DMDM; 74725387; -.
DR MassIVE; Q9P2U7; -.
DR PaxDb; Q9P2U7; -.
DR PeptideAtlas; Q9P2U7; -.
DR PRIDE; Q9P2U7; -.
DR ProteomicsDB; 4105; -.
DR ProteomicsDB; 83898; -. [Q9P2U7-1]
DR TopDownProteomics; Q9P2U7-1; -. [Q9P2U7-1]
DR ABCD; Q9P2U7; 1 sequenced antibody.
DR Antibodypedia; 31998; 246 antibodies from 31 providers.
DR DNASU; 57030; -.
DR Ensembl; ENST00000221485.8; ENSP00000221485.2; ENSG00000104888.10. [Q9P2U7-1]
DR Ensembl; ENST00000600601.5; ENSP00000470338.1; ENSG00000104888.10. [Q9P2U7-2]
DR GeneID; 57030; -.
DR KEGG; hsa:57030; -.
DR MANE-Select; ENST00000221485.8; ENSP00000221485.2; NM_020309.4; NP_064705.1.
DR UCSC; uc002pnp.4; human. [Q9P2U7-1]
DR CTD; 57030; -.
DR DisGeNET; 57030; -.
DR GeneCards; SLC17A7; -.
DR HGNC; HGNC:16704; SLC17A7.
DR HPA; ENSG00000104888; Group enriched (brain, retina).
DR MIM; 605208; gene.
DR neXtProt; NX_Q9P2U7; -.
DR OpenTargets; ENSG00000104888; -.
DR PharmGKB; PA423; -.
DR VEuPathDB; HostDB:ENSG00000104888; -.
DR eggNOG; KOG2532; Eukaryota.
DR GeneTree; ENSGT00940000159110; -.
DR HOGENOM; CLU_001265_5_0_1; -.
DR InParanoid; Q9P2U7; -.
DR OMA; WFPAYLV; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; Q9P2U7; -.
DR TreeFam; TF313535; -.
DR PathwayCommons; Q9P2U7; -.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-428643; Organic anion transporters.
DR SignaLink; Q9P2U7; -.
DR BioGRID-ORCS; 57030; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; SLC17A7; human.
DR GeneWiki; Vesicular_glutamate_transporter_1; -.
DR GenomeRNAi; 57030; -.
DR Pharos; Q9P2U7; Tbio.
DR PRO; PR:Q9P2U7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9P2U7; protein.
DR Bgee; ENSG00000104888; Expressed in right hemisphere of cerebellum and 130 other tissues.
DR ExpressionAtlas; Q9P2U7; baseline and differential.
DR Genevisible; Q9P2U7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0015319; F:sodium:inorganic phosphate symporter activity; IDA:MGI.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; TAS:ProtInc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; ISS:UniProtKB.
DR GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:Reactome.
DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0006817; P:phosphate ion transport; TAS:ProtInc.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; ISS:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiport; Cell membrane; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Ion channel; Ion transport; Membrane;
KW Neurotransmitter transport; Phosphate transport; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..560
FT /note="Vesicular glutamate transporter 1"
FT /id="PRO_0000331611"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 497..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62634"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056110"
FT VAR_SEQ 1..21
FT /note="MEFRQEEFRKLAGRALGKLHR -> MGSQLALAG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056111"
FT VARIANT 431
FT /note="P -> R (in dbSNP:rs17855709)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042904"
SQ SEQUENCE 560 AA; 61613 MW; C88DAFB34B6E45B6 CRC64;
MEFRQEEFRK LAGRALGKLH RLLEKRQEGA ETLELSADGR PVTTQTRDPP VVDCTCFGLP
RRYIIAIMSG LGFCISFGIR CNLGVAIVSM VNNSTTHRGG HVVVQKAQFS WDPETVGLIH
GSFFWGYIVT QIPGGFICQK FAANRVFGFA IVATSTLNML IPSAARVHYG CVIFVRILQG
LVEGVTYPAC HGIWSKWAPP LERSRLATTA FCGSYAGAVV AMPLAGVLVQ YSGWSSVFYV
YGSFGIFWYL FWLLVSYESP ALHPSISEEE RKYIEDAIGE SAKLMNPLTK FSTPWRRFFT
SMPVYAIIVA NFCRSWTFYL LLISQPAYFE EVFGFEISKV GLVSALPHLV MTIIVPIGGQ
IADFLRSRRI MSTTNVRKLM NCGGFGMEAT LLLVVGYSHS KGVAISFLVL AVGFSGFAIS
GFNVNHLDIA PRYASILMGI SNGVGTLSGM VCPIIVGAMT KHKTREEWQY VFLIASLVHY
GGVIFYGVFA SGEKQPWAEP EEMSEEKCGF VGHDQLAGSD DSEMEDEAEP PGAPPAPPPS
YGATHSTFQP PRPPPPVRDY
