SC6A1_MOUSE
ID SC6A1_MOUSE Reviewed; 599 AA.
AC P31648;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sodium- and chloride-dependent GABA transporter 1;
DE Short=GAT-1;
DE AltName: Full=Solute carrier family 6 member 1;
GN Name=Slc6a1; Synonyms=Gabt1, Gat-1, Gat1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1631167; DOI=10.1073/pnas.89.14.6639;
RA Liu Q.-R., Mandiyan S., Nelson H., Nelson N.;
RT "A family of genes encoding neurotransmitter transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6639-6643(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8420981; DOI=10.1016/s0021-9258(18)53968-5;
RA Liu Q.-R., Lopez-Coecuera B., Mandiyan S., Nelson H., Nelson N.;
RT "Molecular characterization of four pharmacologically distinct gamma-
RT aminobutyric acid transporters in mouse brain.";
RL J. Biol. Chem. 268:2106-2112(1993).
RN [4]
RP FUNCTION, TRANSPORTER ACTIVITY, INTERACTION WITH PALS1, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15234345; DOI=10.1016/j.mcn.2004.03.006;
RA McHugh E.M., Zhu W., Milgram S., Mager S.;
RT "The GABA transporter GAT1 and the MAGUK protein Pals1: interaction, uptake
RT modulation, and coexpression in the brain.";
RL Mol. Cell. Neurosci. 26:406-417(2004).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=16150932; DOI=10.1124/mol.105.013870;
RA Krause S., Schwarz W.;
RT "Identification and selective inhibition of the channel mode of the
RT neuronal GABA transporter 1.";
RL Mol. Pharmacol. 68:1728-1735(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=30270321; DOI=10.1248/bpb.b18-00168;
RA Nishimura T., Higuchi K., Yoshida Y., Sugita-Fujisawa Y., Kojima K.,
RA Sugimoto M., Santo M., Tomi M., Nakashima E.;
RT "Hypotaurine Is a Substrate of GABA Transporter Family Members GAT2/Slc6a13
RT and TAUT/Slc6a6.";
RL Biol. Pharm. Bull. 41:1523-1529(2018).
CC -!- FUNCTION: Mediates transport of gamma-aminobutyric acid (GABA) together
CC with sodium and chloride and is responsible for the reuptake of GABA
CC from the synapse (PubMed:15234345, PubMed:16150932, PubMed:8420981,
CC PubMed:30270321). The translocation of GABA, however, may also occur in
CC the reverse direction leading to the release of GABA (By similarity).
CC The direction and magnitude of GABA transport is a consequence of the
CC prevailing thermodynamic conditions, determined by membrane potential
CC and the intracellular and extracellular concentrations of Na(+), Cl(-)
CC and GABA (By similarity). Can also mediate sodium- and chloride-
CC dependent transport of hypotaurine but to a much lower extent as
CC compared to GABA (PubMed:30270321). {ECO:0000250|UniProtKB:P23978,
CC ECO:0000269|PubMed:15234345, ECO:0000269|PubMed:16150932,
CC ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:8420981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:15234345,
CC ECO:0000269|PubMed:16150932, ECO:0000269|PubMed:30270321,
CC ECO:0000269|PubMed:8420981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC Evidence={ECO:0000305|PubMed:15234345};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70689;
CC Evidence={ECO:0000250|UniProtKB:P23978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC Evidence={ECO:0000269|PubMed:30270321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC Evidence={ECO:0000305|PubMed:30270321};
CC -!- ACTIVITY REGULATION: Inhibited by N-[4,4-Diphenyl-3-butenyl]-nipecotic
CC acid (SKF-89976-A), L-2,4-diamino-n-butyric acid, guvacine and
CC nipecotic acid. {ECO:0000269|PubMed:16150932,
CC ECO:0000269|PubMed:8420981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 uM for GABA {ECO:0000269|PubMed:16150932};
CC -!- SUBUNIT: Interacts (via PDZ domain-binding motif) with PALS1;
CC interaction increases SLC6A1-mediated GABA uptake.
CC {ECO:0000269|PubMed:15234345}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23978};
CC Multi-pass membrane protein {ECO:0000255}. Presynapse
CC {ECO:0000269|PubMed:15234345}. Note=Localized at the presynaptic
CC terminals of interneurons. {ECO:0000269|PubMed:15234345}.
CC -!- TISSUE SPECIFICITY: Brain. Expressed in the dentate gyrus of
CC hippocampus, striatum and cerebellum (at protein level).
CC {ECO:0000269|PubMed:15234345}.
CC -!- MISCELLANEOUS: This protein is the target of psychomotor stimulants
CC such as amphetamines or cocaine.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A1 subfamily. {ECO:0000305}.
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DR EMBL; M92377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M92378; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK042956; BAC31418.1; -; mRNA.
DR EMBL; AK052971; BAC35226.1; -; mRNA.
DR EMBL; AK053883; BAC35574.1; -; mRNA.
DR CCDS; CCDS20434.1; -.
DR PIR; F46027; F46027.
DR RefSeq; NP_848818.1; NM_178703.4.
DR AlphaFoldDB; P31648; -.
DR SMR; P31648; -.
DR BioGRID; 231239; 22.
DR IntAct; P31648; 1.
DR MINT; P31648; -.
DR STRING; 10090.ENSMUSP00000032454; -.
DR BindingDB; P31648; -.
DR ChEMBL; CHEMBL5445; -.
DR DrugCentral; P31648; -.
DR GuidetoPHARMACOLOGY; 929; -.
DR GlyGen; P31648; 3 sites.
DR iPTMnet; P31648; -.
DR PhosphoSitePlus; P31648; -.
DR SwissPalm; P31648; -.
DR MaxQB; P31648; -.
DR PaxDb; P31648; -.
DR PeptideAtlas; P31648; -.
DR PRIDE; P31648; -.
DR ProteomicsDB; 256737; -.
DR Antibodypedia; 1391; 270 antibodies from 33 providers.
DR DNASU; 232333; -.
DR Ensembl; ENSMUST00000032454; ENSMUSP00000032454; ENSMUSG00000030310.
DR GeneID; 232333; -.
DR KEGG; mmu:232333; -.
DR UCSC; uc009dhu.2; mouse.
DR CTD; 6529; -.
DR MGI; MGI:95627; Slc6a1.
DR VEuPathDB; HostDB:ENSMUSG00000030310; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000156027; -.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; P31648; -.
DR OMA; GMATFIF; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; P31648; -.
DR TreeFam; TF343812; -.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-MMU-888593; Reuptake of GABA.
DR BioGRID-ORCS; 232333; 4 hits in 74 CRISPR screens.
DR PRO; PR:P31648; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P31648; protein.
DR Bgee; ENSMUSG00000030310; Expressed in cerebellum lobe and 106 other tissues.
DR ExpressionAtlas; P31648; baseline and differential.
DR Genevisible; P31648; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015378; F:sodium:chloride symporter activity; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IMP:ARUK-UCL.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR GO; GO:0051939; P:gamma-aminobutyric acid import; IMP:ARUK-UCL.
DR GO; GO:0098658; P:inorganic anion import across plasma membrane; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:ARUK-UCL.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:MGI.
DR GO; GO:0098810; P:neurotransmitter reuptake; ISO:MGI.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0010035; P:response to inorganic substance; ISO:MGI.
DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0014074; P:response to purine-containing compound; ISO:MGI.
DR GO; GO:0009744; P:response to sucrose; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IMP:ARUK-UCL.
DR CDD; cd11506; SLC6sbd_GAT1; 1.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002980; Na/ntran_symport_GABA_GAT1.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR01195; GAT1TRNSPORT.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Sodium; Symport; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..599
FT /note="Sodium- and chloride-dependent GABA transporter 1"
FT /id="PRO_0000214744"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 53..73
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..80
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 81..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 124..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..211
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 212..230
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 239..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..291
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 292..309
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 321..342
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..374
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 375..394
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 422..440
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 457..477
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 498..517
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..535
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT TRANSMEM 536..554
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..599
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23978"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..599
FT /note="PDZ-binding"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 61
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 62
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 66
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 295
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 327
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 392
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 395
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 396
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..173
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CONFLICT 117..118
FT /note="KL -> NW (in Ref. 1; M92378)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..127
FT /note="GL -> AV (in Ref. 1; M92378)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..213
FT /note="WP -> C (in Ref. 1; M92378)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="WL -> IF (in Ref. 1; M92378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67001 MW; 4FEF85092DC1D045 CRC64;
MATDNSKVAD GQISTEVSEA PVASDKPKTL VVKVQKKAGD LPDRDTWKGR FDFLMSCVGY
AIGLGNVWRF PYLCGKNGGG AFLIPYFLTL IFAGVPLFLL ECSLGQYTSI GGLGVWKLAP
MFKGVGLAAA VLSFWLNIYY IVIISWAIYY LYNSFTTTLP WKQCDNPWNT DRCFSNYSLV
NTTNMTSAVV EFWERNMHQM TDGLDKPGQI RWPLAITLAI AWVLVYFCIW KGVGWTGKVV
YFSATYPYIM LIILFFRGVT LPGAKEGILF YITPNFRKLS DSEVWLDAAT QIFFSYGLGL
GSLIALGSYN SFHNNVYRDS IIVCCINSCT SMFAGFVIFS IVGFMAHVTK RSIADVAASG
PGLAFLAYPE AVTQLPISPL WAILFFSMLL MLGIDSQFCT VEGFITALVD EYPRLLRNRR
ELFIAAVCIV SYLIGLSNIT QGGIYVFKLF DYYSASGMSL LFLVFFECVS ISWFYGVNRF
YDNIQEMVGS RPCIWWKLCW SFFTPIIVAG VFLFSAVQMT PLTMGSYVFP KWGQGVGWLM
ALSSMVLIPG YMAYMFLTLK GSLKQRLQVM IQPSEDIVRP ENGPEQPQAG SSASKEAYI
