NMDZ1_XENLA
ID NMDZ1_XENLA Reviewed; 903 AA.
AC A0A1L8F5J9; C0KD15; C0KD16; C0KD17; C0KD18; C0KD19; Q4PLR7; Q91805; Q91977;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 1;
DE Short=GluN1;
DE AltName: Full=N-methyl-D-aspartate receptor subunit NR1 {ECO:0000303|PubMed:16214956};
DE Short=NMD-R1;
DE Flags: Precursor;
GN Name=grin1 {ECO:0000312|Xenbase:XB-GENE-866327};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|Proteomes:UP000186698};
RN [1] {ECO:0000312|EMBL:CAA63825.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND SUBCELLULAR LOCATION.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA63825.1};
RX PubMed=8975675;
RA Soloviev M.M., Ishimaru H., Barnard E.A.;
RT "A new type of ionotropic glutamate receptors.";
RL Bioorg. Khim. 22:468-471(1996).
RN [2] {ECO:0000312|EMBL:CAA63871.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND SUBCELLULAR LOCATION.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA63871.1};
RX PubMed=8955083; DOI=10.1074/jbc.271.51.32572;
RA Soloviev M.M., Brierley M.J., Shao Z.Y., Mellor I.R., Volkova T.M.,
RA Kamboj R., Ishimaru H., Sudan H., Harris J., Foldes R.L., Grishin E.V.,
RA Usherwood P.N.R., Barnard E.A.;
RT "Functional expression of a recombinant unitary glutamate receptor from
RT Xenopus, which contains N-methyl-D-aspartate (NMDA) and non-NMDA receptor
RT subunits.";
RL J. Biol. Chem. 271:32572-32579(1996).
RN [3] {ECO:0000312|EMBL:AAY63890.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=16214956; DOI=10.1124/mol.105.016840;
RA Schmidt C., Werner M., Hollmann M.;
RT "Revisiting the postulated 'unitary glutamate receptor':
RT electrophysiological and pharmacological analysis in two heterologous
RT expression systems fails to detect evidence for its existence.";
RL Mol. Pharmacol. 69:119-129(2006).
RN [4] {ECO:0000312|EMBL:ACN87989.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Brain {ECO:0000312|EMBL:ACN87989.1};
RX PubMed=19524674; DOI=10.1016/j.mcn.2009.06.004;
RA Schmidt C., Hollmann M.;
RT "Molecular and functional characterization of Xenopus laevis N-methyl-d-
RT aspartate receptors.";
RL Mol. Cell. Neurosci. 42:116-127(2009).
RN [5] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [6] {ECO:0007744|PDB:3QEK, ECO:0007744|PDB:3QEL, ECO:0007744|PDB:3QEM}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 23-405 IN COMPLEX WITH GRIN2B,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-276; ASN-300
RP AND ASN-368, AND DISULFIDE BONDS.
RX PubMed=21677647; DOI=10.1038/nature10180;
RA Karakas E., Simorowski N., Furukawa H.;
RT "Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA
RT receptors.";
RL Nature 475:249-253(2011).
RN [7] {ECO:0007744|PDB:4TLL, ECO:0007744|PDB:4TLM}
RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 22-836 IN COMPLEX WITH GRIN2B,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, GLYCOSYLATION AT ASN-61;
RP ASN-203 AND ASN-276, AND DISULFIDE BONDS.
RX PubMed=25008524; DOI=10.1038/nature13548;
RA Lee C.H., Lu W., Michel J.C., Goehring A., Du J., Song X., Gouaux E.;
RT "NMDA receptor structures reveal subunit arrangement and pore
RT architecture.";
RL Nature 511:191-197(2014).
RN [8] {ECO:0007744|PDB:5IOU, ECO:0007744|PDB:5IOV, ECO:0007744|PDB:5IPQ}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS) OF 23-836 IN COMPLEX WITH
RP GRIN2B, TOPOLOGY, AND SUBUNIT.
RX PubMed=27062927; DOI=10.1016/j.cell.2016.03.028;
RA Zhu S., Stein R.A., Yoshioka C., Lee C.H., Goehring A., Mchaourab H.S.,
RA Gouaux E.;
RT "Mechanism of NMDA Receptor Inhibition and Activation.";
RL Cell 165:704-714(2016).
RN [9] {ECO:0007744|PDB:5EWJ, ECO:0007744|PDB:5EWL, ECO:0007744|PDB:5EWM}
RP X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 23-408 IN COMPLEX WITH GRIN2B,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=26912815; DOI=10.1124/mol.115.103036;
RA Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M., Sciabola S.,
RA Mony L., Paoletti P., Pandit J.;
RT "A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-
RT selective Antagonists.";
RL Mol. Pharmacol. 89:541-551(2016).
RN [10] {ECO:0007744|PDB:5B3J}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 23-405 IN COMPLEX WITH GRIN2B,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=27135925; DOI=10.1038/nature17679;
RA Tajima N., Karakas E., Grant T., Simorowski N., Diaz-Avalos R.,
RA Grigorieff N., Furukawa H.;
RT "Activation of NMDA receptors and the mechanism of inhibition by
RT ifenprodil.";
RL Nature 534:63-68(2016).
RN [11] {ECO:0007744|PDB:5TPW, ECO:0007744|PDB:5TPZ, ECO:0007744|PDB:5TQ0}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-408 IN COMPLEX WITH ZINC IONS
RP AND GRIN2A, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT,
RP GLYCOSYLATION AT ASN-203 AND ASN-300, AND DISULFIDE BONDS.
RX DOI=10.1016/j.neuron.2016.11.006;
RA Romero-Hernandez A., Simorowski N., Karakas E., Furukawa H.;
RT "Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition
RT in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.";
RL Neuron 92:1-13(2016).
RN [12] {ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-836 IN COMPLEX WITH
RP GRIN2A AND GRIN2B, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, DOMAIN,
RP GLYCOSYLATION AT ASN-61; ASN-203 AND ASN-276, AND DISULFIDE BONDS.
RX PubMed=28232581; DOI=10.1126/science.aal3729;
RA Lu W., Du J., Goehring A., Gouaux E.;
RT "Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric
RT modulation.";
RL Science 355:0-0(2017).
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+)
CC (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524,
CC PubMed:26912815, PubMed:27135925, Ref.11, PubMed:28232581). Sensitivity
CC to glutamate and channel kinetics depend on the subunit composition
CC (Probable). {ECO:0000269|PubMed:16214956, ECO:0000269|PubMed:19524674,
CC ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524,
CC ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Channel activity is modulated by zinc ions. The
CC activity of the heterotetramer with grin2b is stimulated by micromolar
CC levels of Zn(2+) (PubMed:19524674). The activity of the heterotetramer
CC with grin2a is inhibited by nanomolar levels of Zn(2+) (Ref.11).
CC {ECO:0000269|PubMed:19524674, ECO:0000269|Ref.11}.
CC -!- SUBUNIT: Heterotetramer (PubMed:27062927). Forms heterotetrameric
CC channels composed of two zeta subunits (grin1), and two epsilon
CC subunits (grin2a, grin2b, grin2c or grin2d) (in vitro)
CC (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524,
CC PubMed:26912815, PubMed:27135925, Ref.11, PubMed:28232581). Does not
CC form functional channels by itself (PubMed:16214956). In vivo, the
CC subunit composition may depend on the expression levels of the
CC different subunits (Probable). {ECO:0000269|PubMed:16214956,
CC ECO:0000269|PubMed:19524674, ECO:0000269|PubMed:21677647,
CC ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:26912815,
CC ECO:0000269|PubMed:27062927, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11, ECO:0000305}.
CC -!- INTERACTION:
CC A0A1L8F5J9; A7XY94: grin2b; NbExp=3; IntAct=EBI-15932423, EBI-16113306;
CC A0A1L8F5J9-8; Q00960: Grin2b; Xeno; NbExp=6; IntAct=EBI-16582829, EBI-396905;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19524674,
CC ECO:0000269|PubMed:21677647, ECO:0000269|PubMed:25008524,
CC ECO:0000269|PubMed:26912815, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:27062927,
CC ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane
CC {ECO:0000305|PubMed:8955083, ECO:0000305|PubMed:8975675}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane
CC {ECO:0000269|PubMed:16214956}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=A0A1L8F5J9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1L8F5J9-2; Sequence=VSP_059211;
CC Name=3;
CC IsoId=A0A1L8F5J9-3; Sequence=VSP_059207, VSP_059211;
CC Name=4;
CC IsoId=A0A1L8F5J9-4; Sequence=VSP_059209, VSP_059210;
CC Name=5;
CC IsoId=A0A1L8F5J9-5; Sequence=VSP_059207, VSP_059209, VSP_059210;
CC Name=6;
CC IsoId=A0A1L8F5J9-6; Sequence=VSP_059207, VSP_059208;
CC Name=7;
CC IsoId=A0A1L8F5J9-7; Sequence=VSP_059208;
CC Name=8;
CC IsoId=A0A1L8F5J9-8; Sequence=VSP_059206, VSP_059208;
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000305|PubMed:25008524, ECO:0000305|PubMed:28232581}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR1/GRIN1 subfamily. {ECO:0000305}.
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DR EMBL; X94081; CAA63825.1; -; mRNA.
DR EMBL; X94156; CAA63871.1; -; mRNA.
DR EMBL; DQ066918; AAY63890.1; -; mRNA.
DR EMBL; FJ571597; ACN87989.1; -; mRNA.
DR EMBL; FJ571598; ACN87990.1; -; mRNA.
DR EMBL; FJ571599; ACN87991.1; -; mRNA.
DR EMBL; FJ571600; ACN87992.1; -; mRNA.
DR EMBL; FJ571601; ACN87993.1; -; mRNA.
DR EMBL; CM004480; OCT66859.1; -; Genomic_DNA.
DR RefSeq; NP_001081615.1; NM_001088146.1. [A0A1L8F5J9-8]
DR RefSeq; NP_001081616.1; NM_001088147.1. [A0A1L8F5J9-7]
DR PDB; 3QEK; X-ray; 2.00 A; A/B=23-384.
DR PDB; 3QEL; X-ray; 2.60 A; A/C=23-384.
DR PDB; 3QEM; X-ray; 3.00 A; A/C=23-384.
DR PDB; 4TLL; X-ray; 3.59 A; A/C=22-836.
DR PDB; 4TLM; X-ray; 3.77 A; A/C=22-836.
DR PDB; 5B3J; X-ray; 2.90 A; A/B=23-384.
DR PDB; 5EWJ; X-ray; 2.77 A; A/C=23-387.
DR PDB; 5EWL; X-ray; 2.98 A; A/C=23-387.
DR PDB; 5EWM; X-ray; 2.76 A; A/C=23-387.
DR PDB; 5IOU; EM; 7.00 A; A/C=23-836.
DR PDB; 5IOV; EM; 7.50 A; A/C=23-836.
DR PDB; 5IPQ; EM; 13.50 A; A/C=23-836.
DR PDB; 5IPR; EM; 14.10 A; A/C=23-836.
DR PDB; 5IPS; EM; 13.50 A; A/C=23-836.
DR PDB; 5IPT; EM; 14.10 A; A/C=23-836.
DR PDB; 5IPU; EM; 15.40 A; A/C=23-836.
DR PDB; 5IPV; EM; 9.25 A; A/C=23-836.
DR PDB; 5TPW; X-ray; 2.91 A; A=24-387.
DR PDB; 5TPZ; X-ray; 3.10 A; A=23-384.
DR PDB; 5TQ0; X-ray; 2.70 A; A=24-387.
DR PDB; 5TQ2; X-ray; 3.29 A; A=24-387.
DR PDB; 5UN1; X-ray; 3.60 A; A/C/E/G=394-836.
DR PDB; 5UOW; EM; 4.50 A; A/C=23-836.
DR PDB; 5UP2; EM; 6.00 A; A/C=1-836.
DR PDB; 6E7R; X-ray; 2.10 A; A/C=23-386.
DR PDB; 6E7S; X-ray; 2.72 A; A/C=23-386.
DR PDB; 6E7T; X-ray; 2.31 A; A/C=23-386.
DR PDB; 6E7U; X-ray; 2.27 A; A/C=23-386.
DR PDB; 6E7V; X-ray; 2.60 A; A/C=23-386.
DR PDB; 6E7W; X-ray; 2.67 A; A/C=23-386.
DR PDB; 6E7X; X-ray; 2.58 A; A/C=23-386.
DR PDB; 7TE6; X-ray; 4.55 A; A/E=23-384.
DR PDBsum; 3QEK; -.
DR PDBsum; 3QEL; -.
DR PDBsum; 3QEM; -.
DR PDBsum; 4TLL; -.
DR PDBsum; 4TLM; -.
DR PDBsum; 5B3J; -.
DR PDBsum; 5EWJ; -.
DR PDBsum; 5EWL; -.
DR PDBsum; 5EWM; -.
DR PDBsum; 5IOU; -.
DR PDBsum; 5IOV; -.
DR PDBsum; 5IPQ; -.
DR PDBsum; 5IPR; -.
DR PDBsum; 5IPS; -.
DR PDBsum; 5IPT; -.
DR PDBsum; 5IPU; -.
DR PDBsum; 5IPV; -.
DR PDBsum; 5TPW; -.
DR PDBsum; 5TPZ; -.
DR PDBsum; 5TQ0; -.
DR PDBsum; 5TQ2; -.
DR PDBsum; 5UN1; -.
DR PDBsum; 5UOW; -.
DR PDBsum; 5UP2; -.
DR PDBsum; 6E7R; -.
DR PDBsum; 6E7S; -.
DR PDBsum; 6E7T; -.
DR PDBsum; 6E7U; -.
DR PDBsum; 6E7V; -.
DR PDBsum; 6E7W; -.
DR PDBsum; 6E7X; -.
DR PDBsum; 7TE6; -.
DR AlphaFoldDB; A0A1L8F5J9; -.
DR SMR; A0A1L8F5J9; -.
DR DIP; DIP-59169N; -.
DR DIP; DIP-61036N; -.
DR IntAct; A0A1L8F5J9; 2.
DR STRING; 8355.A0A1L8F5J9; -.
DR TCDB; 1.A.10.1.12; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR iPTMnet; A0A1L8F5J9; -.
DR ABCD; A0A1L8F5J9; 1 sequenced antibody.
DR GeneID; 397953; -.
DR KEGG; xla:397953; -.
DR CTD; 397953; -.
DR Xenbase; XB-GENE-866327; grin1.L.
DR OrthoDB; 188544at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 397953; Expressed in brain and 10 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IDA:UniProtKB.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10562; CaM_bdg_C0; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Metal-binding; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..903
FT /note="Glutamate receptor ionotropic, NMDA 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000442209"
FT TOPO_DOM 21..557
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 579..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 601..622
FT /note="Discontinuously helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 623..628
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 629..645
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 646..810
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:25008524"
FT TOPO_DOM 832..903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 601..620
FT /note="Pore-forming"
FT /evidence="ECO:0000305|PubMed:25008524"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.11"
FT BINDING 514..516
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 521
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 686
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 730
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:5UOW"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25008524,
FT ECO:0000269|PubMed:28232581, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:4TLL, ECO:0007744|PDB:5TPZ,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21677647,
FT ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581,
FT ECO:0007744|PDB:3QEK, ECO:0007744|PDB:3QEL,
FT ECO:0007744|PDB:3QEM, ECO:0007744|PDB:4TLL,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21677647, ECO:0000269|Ref.11,
FT ECO:0007744|PDB:3QEK, ECO:0007744|PDB:5TPZ"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21677647,
FT ECO:0007744|PDB:3QEK, ECO:0007744|PDB:3QEL,
FT ECO:0007744|PDB:3QEM"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 79..308
FT /evidence="ECO:0000269|PubMed:28232581,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT DISULFID 420..452
FT /evidence="ECO:0000269|PubMed:28232581,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT DISULFID 436..453
FT /evidence="ECO:0000269|PubMed:28232581,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT DISULFID 742..796
FT /evidence="ECO:0000269|PubMed:28232581,
FT ECO:0007744|PDB:5UOW, ECO:0007744|PDB:5UP2"
FT VAR_SEQ 186..189
FT /note="EKES -> GKESKSKKRNYENLDQLSYDNKRGP (in isoform 8)"
FT /id="VSP_059206"
FT VAR_SEQ 189
FT /note="S -> SKSKKRNYENLDQLSYDNKRGP (in isoform 3, isoform 5
FT and isoform 6)"
FT /id="VSP_059207"
FT VAR_SEQ 862..901
FT /note="DRKSGRAEPDPKKKASFRSITSTLASSFKRRRSSKDTVNV -> QYPPTDIT
FT GQLNLSDPSVST (in isoform 6, isoform 7 and isoform 8)"
FT /id="VSP_059208"
FT VAR_SEQ 862..866
FT /note="DRKSG -> PGNIK (in isoform 4 and isoform 5)"
FT /id="VSP_059209"
FT VAR_SEQ 867..903
FT /note="Missing (in isoform 4 and isoform 5)"
FT /id="VSP_059210"
FT VAR_SEQ 899..901
FT /note="VNV -> QYPPTDITGQLNLSDPSVST (in isoform 2 and
FT isoform 3)"
FT /id="VSP_059211"
FT STRAND 25..35
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5TQ2"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5TQ2"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:3QEK"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6E7U"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5TQ2"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3QEK"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:3QEK"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6E7R"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:6E7R"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:3QEK"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5TQ0"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:5TQ0"
SQ SEQUENCE 903 AA; 101793 MW; E2612938C9125D76 CRC64;
MGTMRLFLLA VLFLFSFARA GCDPKIVNIG AVLSTKKHEQ IFREAVNQAN KRHFTRKIQL
NATSVTHRPN AIQMALSVCE DLISSQVYAI LVSHPPAPTD HLTPTPISYT AGFYRIPVIG
LTTRMSIYSD KSIHLSFLRT VPPYSHQALV WFEMMRLFNW NHVILIVSDD HEGRAAQKKL
ETLLEEKESK ADKVLQFEPG TKNLTALLLE AKELEARVII LSASEDDATA VYKSAAMLDM
TGAGYVWLVG EREISGSALR YAPDGIIGLQ LINGKNESAH ISDAVAVVAQ AIHELFEMEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY PDGVTGRIEF NEDGDRKFAN YSIMNLQNRK
LVQVGIFNGS YIIQNDRKII WPGGETERPQ GYQMSTRLKI VTIHQEPFVY VRPTTSDGTC
REEYTINGDP IKKVICNGPN ETIPGRPTVP QCCYGFCVDL LIKLAREMNF TYEVHLVADG
KFGTQERVNN SNKKEWNGMM GELLSGQADM IVAPLTINNE RAQYIEFSKP FKYQGLTILV
KKEIPRSTLD SFMQPFQSTL WLLVGLSVHV VAVMLYLLDR FSPFGRFKVN SEEEEEDALT
LSSAMWFSWG VLLNSGIGEG APRSFSARIL GMVWAGFAMI IVASYTANLA AFLVLDRPEE
RITGINDPRL RNPSDKFIYA TVKQSSVDIY FRRQVELSTM YRHMEKHNYE SAAEAIQAVR
DNKLHAFIWD SAVLEFEASQ KCDLVTTGEL FFRSGFGIGM RKDSPWKQNV SLNILKSHEN
GFMEELDKTW VRYQECDSRS NAPATLTFEN MAGVFMLVAG GIVAGIFLIF IEIAYKRHKD
ARRKQMQLAF AAVNVWRKNL QDRKSGRAEP DPKKKASFRS ITSTLASSFK RRRSSKDTVN
VVV
