PANX1_HUMAN
ID PANX1_HUMAN Reviewed; 426 AA.
AC Q96RD7; O75968; Q543A0; Q6UW26; Q96AM9; Q96L77; Q96RS5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Pannexin-1;
GN Name=PANX1 {ECO:0000312|HGNC:HGNC:8599}; Synonyms=MRS1;
GN ORFNames=UNQ2529/PRO6028;
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 2), AND VARIANT HIS-5.
RA Bolger G.B., Steele M.R.;
RT "A novel cDNA of unknown function.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND VARIANT HIS-5.
RX PubMed=15028292; DOI=10.1016/j.ygeno.2003.09.025;
RA Baranova A., Ivanov D., Petrash N., Pestova A., Skoblov M., Kelmanson I.,
RA Shagin D., Nazarenko S., Geraymovych E., Litvin O., Tiunova A., Born T.L.,
RA Usman N., Staroverov D., Lukyanov S., Panchin Y.;
RT "The mammalian pannexin family is homologous to the invertebrate innexin
RT gap junction proteins.";
RL Genomics 83:706-716(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-5.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-5.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-426.
RA Baranova A.V., Ivanov D.V., Borodina T.A., Panchin Y.V., Shagin D.A.,
RA Lukyanov S.A.;
RT "Genomic organization of putative human gap junction proteins PANX1 and
RT PANX2.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16908669; DOI=10.1083/jcb.200601115;
RA Vanden Abeele F., Bidaux G., Gordienko D., Beck B., Panchin Y.V.,
RA Baranova A.V., Ivanov D.V., Skryma R., Prevarskaya N.;
RT "Functional implications of calcium permeability of the channel formed by
RT pannexin 1.";
RL J. Cell Biol. 174:535-546(2006).
RN [9]
RP GLYCOSYLATION AT ASN-255, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASN-255.
RX PubMed=17715132; DOI=10.1074/jbc.m702422200;
RA Boassa D., Ambrosi C., Qiu F., Dahl G., Gaietta G., Sosinsky G.;
RT "Pannexin1 channels contain a glycosylation site that targets the hexamer
RT to the plasma membrane.";
RL J. Biol. Chem. 282:31733-31743(2007).
RN [10]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT OOMD7 SER-347.
RX PubMed=20829356; DOI=10.1074/jbc.m110.101014;
RA Bunse S., Schmidt M., Prochnow N., Zoidl G., Dermietzel R.;
RT "Intracellular cysteine 346 is essentially involved in regulating Panx1
RT channel activity.";
RL J. Biol. Chem. 285:38444-38452(2010).
RN [11]
RP VARIANT HIS-217, AND CHARACTERIZATION OF VARIANT HIS-217.
RX PubMed=27129271; DOI=10.1074/jbc.m116.717934;
RA Shao Q., Lindstrom K., Shi R., Kelly J., Schroeder A., Juusola J.,
RA Levine K.L., Esseltine J.L., Penuela S., Jackson M.F., Laird D.W.;
RT "A Germline Variant in the PANX1 Gene Has Reduced Channel Function and Is
RT Associated with Multisystem Dysfunction.";
RL J. Biol. Chem. 291:12432-12443(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN OOMD7,
RP VARIANTS OOMD7 21-THR--PRO-23 DEL; GLU-346; SER-347 AND 392-GLN--CYS-426
RP DEL, CHARACTERIZATION OF VARIANTS OOMD7 21-THR--PRO-23 DEL; GLU-346;
RP SER-347 AND 392-GLN--CYS-426 DEL, MUTAGENESIS OF ASN-255; ASN-338 AND
RP ASN-394, VARIANTS HIS-217 AND VAL-272, CHARACTERIZATION OF VARIANTS HIS-217
RP AND VAL-272, AND GLYCOSYLATION.
RX PubMed=30918116; DOI=10.1126/scitranslmed.aav8731;
RA Sang Q., Zhang Z., Shi J., Sun X., Li B., Yan Z., Xue S., Ai A., Lyu Q.,
RA Li W., Zhang J., Wu L., Mao X., Chen B., Mu J., Li Q., Du J., Sun Q.,
RA Jin L., He L., Zhu S., Kuang Y., Wang L.;
RT "A pannexin 1 channelopathy causes human oocyte death.";
RL Sci. Transl. Med. 11:0-0(2019).
CC -!- FUNCTION: Structural component of the gap junctions and the
CC hemichannels involved in the ATP release and nucleotide permeation
CC (PubMed:16908669, PubMed:20829356, PubMed:30918116). May play a role as
CC a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis
CC (PubMed:16908669). Plays a critical role in oogenesis
CC (PubMed:30918116). {ECO:0000269|PubMed:16908669,
CC ECO:0000269|PubMed:20829356, ECO:0000269|PubMed:30918116}.
CC -!- SUBUNIT: Homohexamer. Forms homomeric or PANX1/PANX2-heteromeric
CC intercellular channels on coexpression in paired Xenopus oocytes (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96RD7; P02652: APOA2; NbExp=3; IntAct=EBI-7037612, EBI-1171525;
CC Q96RD7; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-7037612, EBI-4290634;
CC Q96RD7; P41181: AQP2; NbExp=3; IntAct=EBI-7037612, EBI-12701138;
CC Q96RD7; Q92843: BCL2L2; NbExp=3; IntAct=EBI-7037612, EBI-707714;
CC Q96RD7; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-7037612, EBI-11579371;
CC Q96RD7; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-7037612, EBI-12142299;
CC Q96RD7; P37268: FDFT1; NbExp=3; IntAct=EBI-7037612, EBI-714550;
CC Q96RD7; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-7037612, EBI-10314552;
CC Q96RD7; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-7037612, EBI-12195227;
CC Q96RD7; P01375: TNF; NbExp=3; IntAct=EBI-7037612, EBI-359977;
CC Q96RD7; O95183: VAMP5; NbExp=3; IntAct=EBI-7037612, EBI-10191195;
CC Q96RD7; Q14508: WFDC2; NbExp=3; IntAct=EBI-7037612, EBI-723529;
CC Q96RD7-1; Q96RD7-1: PANX1; NbExp=4; IntAct=EBI-25747443, EBI-25747443;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30918116};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
CC Cell junction, gap junction {ECO:0000269|PubMed:16908669,
CC ECO:0000269|PubMed:17715132}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96RD7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RD7-2; Sequence=VSP_011476;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:30918116). Highest
CC expression is observed in oocytes and brain (PubMed:30918116). Detected
CC at very low levels in sperm cells (PubMed:30918116).
CC {ECO:0000269|PubMed:30918116}.
CC -!- PTM: S-nitrosylation inhibits channel currents and ATP release.
CC {ECO:0000250|UniProtKB:Q9JIP4}.
CC -!- PTM: N-glycosylation may play a role in cell surface targeting (By
CC similarity). Exists in three glycosylation states: non-glycosylated
CC (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated
CC (GLY2) (PubMed:30918116). {ECO:0000250|UniProtKB:Q9JIP4,
CC ECO:0000269|PubMed:30918116}.
CC -!- DISEASE: Oocyte maturation defect 7 (OOMD7) [MIM:618550]: An autosomal
CC dominant infertility disorder due to oocyte degeneration and death,
CC which may occur before or after fertilization.
CC {ECO:0000269|PubMed:20829356, ECO:0000269|PubMed:30918116}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Pannexin entry;
CC URL="https://en.wikipedia.org/wiki/Pannexin";
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; AF093239; AAC61779.1; -; mRNA.
DR EMBL; AF398509; AAK91714.1; -; mRNA.
DR EMBL; AF398508; AAK91713.1; -; Genomic_DNA.
DR EMBL; AF398506; AAK91713.1; JOINED; Genomic_DNA.
DR EMBL; AF398507; AAK91713.1; JOINED; Genomic_DNA.
DR EMBL; AY048509; AAL06604.1; -; Genomic_DNA.
DR EMBL; AY359023; AAQ89382.1; -; mRNA.
DR EMBL; AK074897; BAC11276.1; -; mRNA.
DR EMBL; AP003966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016931; AAH16931.1; -; mRNA.
DR EMBL; AH010945; AAK73361.1; -; Genomic_DNA.
DR CCDS; CCDS8296.1; -. [Q96RD7-1]
DR RefSeq; NP_056183.2; NM_015368.3. [Q96RD7-1]
DR PDB; 6LTN; EM; 3.10 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6LTO; EM; 3.10 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6M02; EM; 3.20 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6M66; EM; 4.10 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6M67; EM; 3.60 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6M68; EM; 4.60 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6V6D; EM; 3.77 A; A/B/C/D/E/F/G=1-426.
DR PDB; 6WBF; EM; 2.83 A; A/B/C/D/E/F/G=1-373.
DR PDB; 6WBG; EM; 2.97 A; A/B/C/D/E/F/G=1-373.
DR PDB; 6WBI; EM; 4.39 A; A/B/C/D/E/F/G=1-371.
DR PDB; 6WBK; EM; 6.01 A; A/B/C/D/E/F/G=1-370.
DR PDB; 6WBL; EM; 5.13 A; A/B/C/D/E/F/G=1-370.
DR PDB; 6WBM; EM; 2.86 A; A/B/C/D/E/F/G=1-373.
DR PDB; 6WBN; EM; 2.83 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-373.
DR PDB; 7DWB; EM; 3.15 A; A/B/C/D/E/F/G=2-426.
DR PDB; 7F8J; EM; 3.60 A; A/B/C/D/E/F/G=1-426.
DR PDB; 7F8N; EM; 3.40 A; A/B/C/D/E/F/G=1-426.
DR PDB; 7F8O; EM; 3.60 A; A/B/C/D/E/F/G=1-426.
DR PDB; 7WSV; EM; 4.50 A; A/B/C/D/E/F/G=21-426.
DR PDBsum; 6LTN; -.
DR PDBsum; 6LTO; -.
DR PDBsum; 6M02; -.
DR PDBsum; 6M66; -.
DR PDBsum; 6M67; -.
DR PDBsum; 6M68; -.
DR PDBsum; 6V6D; -.
DR PDBsum; 6WBF; -.
DR PDBsum; 6WBG; -.
DR PDBsum; 6WBI; -.
DR PDBsum; 6WBK; -.
DR PDBsum; 6WBL; -.
DR PDBsum; 6WBM; -.
DR PDBsum; 6WBN; -.
DR PDBsum; 7DWB; -.
DR PDBsum; 7F8J; -.
DR PDBsum; 7F8N; -.
DR PDBsum; 7F8O; -.
DR PDBsum; 7WSV; -.
DR AlphaFoldDB; Q96RD7; -.
DR SMR; Q96RD7; -.
DR BioGRID; 117295; 298.
DR DIP; DIP-43936N; -.
DR IntAct; Q96RD7; 27.
DR MINT; Q96RD7; -.
DR STRING; 9606.ENSP00000227638; -.
DR BindingDB; Q96RD7; -.
DR ChEMBL; CHEMBL3779756; -.
DR DrugBank; DB01032; Probenecid.
DR TCDB; 1.A.25.2.1; the gap junction-forming innexin (innexin) family.
DR GlyGen; Q96RD7; 1 site.
DR iPTMnet; Q96RD7; -.
DR PhosphoSitePlus; Q96RD7; -.
DR BioMuta; PANX1; -.
DR DMDM; 317373551; -.
DR EPD; Q96RD7; -.
DR jPOST; Q96RD7; -.
DR MassIVE; Q96RD7; -.
DR MaxQB; Q96RD7; -.
DR PaxDb; Q96RD7; -.
DR PeptideAtlas; Q96RD7; -.
DR PRIDE; Q96RD7; -.
DR ProteomicsDB; 77946; -. [Q96RD7-1]
DR ProteomicsDB; 77947; -. [Q96RD7-2]
DR ABCD; Q96RD7; 1 sequenced antibody.
DR Antibodypedia; 1920; 263 antibodies from 38 providers.
DR DNASU; 24145; -.
DR Ensembl; ENST00000227638.8; ENSP00000227638.3; ENSG00000110218.9. [Q96RD7-1]
DR Ensembl; ENST00000436171.2; ENSP00000411461.2; ENSG00000110218.9. [Q96RD7-2]
DR GeneID; 24145; -.
DR KEGG; hsa:24145; -.
DR MANE-Select; ENST00000227638.8; ENSP00000227638.3; NM_015368.4; NP_056183.2.
DR UCSC; uc001peq.4; human. [Q96RD7-1]
DR CTD; 24145; -.
DR DisGeNET; 24145; -.
DR GeneCards; PANX1; -.
DR HGNC; HGNC:8599; PANX1.
DR HPA; ENSG00000110218; Low tissue specificity.
DR MalaCards; PANX1; -.
DR MIM; 608420; gene.
DR MIM; 618550; phenotype.
DR neXtProt; NX_Q96RD7; -.
DR OpenTargets; ENSG00000110218; -.
DR Orphanet; 488191; Female infertility due to oocyte meiotic arrest.
DR PharmGKB; PA32929; -.
DR VEuPathDB; HostDB:ENSG00000110218; -.
DR eggNOG; ENOG502QT58; Eukaryota.
DR GeneTree; ENSGT00940000153972; -.
DR HOGENOM; CLU_050054_1_0_1; -.
DR InParanoid; Q96RD7; -.
DR OMA; IPDRFQC; -.
DR PhylomeDB; Q96RD7; -.
DR TreeFam; TF333142; -.
DR PathwayCommons; Q96RD7; -.
DR Reactome; R-HSA-112303; Electric Transmission Across Gap Junctions.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR SignaLink; Q96RD7; -.
DR BioGRID-ORCS; 24145; 10 hits in 1086 CRISPR screens.
DR ChiTaRS; PANX1; human.
DR GeneWiki; PANX1; -.
DR GenomeRNAi; 24145; -.
DR Pharos; Q96RD7; Tbio.
DR PRO; PR:Q96RD7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96RD7; protein.
DR Bgee; ENSG00000110218; Expressed in cortical plate and 141 other tissues.
DR ExpressionAtlas; Q96RD7; baseline and differential.
DR Genevisible; Q96RD7; HS.
DR GO; GO:0032059; C:bleb; IDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0022840; F:leak channel activity; IMP:UniProtKB.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0022829; F:wide pore channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IMP:UniProtKB.
DR GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR DisProt; DP02945; -.
DR InterPro; IPR000990; Innexin.
DR InterPro; IPR039099; Pannexin.
DR PANTHER; PTHR15759; PTHR15759; 1.
DR Pfam; PF00876; Innexin; 1.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Cell junction; Cell membrane; Differentiation;
KW Disease variant; Endoplasmic reticulum; Gap junction; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Oogenesis; Reference proteome;
KW S-nitrosylation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Pannexin-1"
FT /id="PRO_0000208484"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 62..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 128..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 239..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 288..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT MOD_RES 347
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17715132,
FT ECO:0000269|PubMed:30918116"
FT VAR_SEQ 401..404
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15028292, ECO:0000303|Ref.1"
FT /id="VSP_011476"
FT VARIANT 5
FT /note="Q -> H (in dbSNP:rs1138800)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15028292, ECO:0000269|PubMed:16303743,
FT ECO:0000269|Ref.1"
FT /id="VAR_016098"
FT VARIANT 21..23
FT /note="Missing (in OOMD7; impaired glycosylation resulting
FT in the absence of GLY2 and the accumulation of GLY1 forms;
FT associated with increased hemi-channel activity)"
FT /evidence="ECO:0000269|PubMed:30918116"
FT /id="VAR_083161"
FT VARIANT 217
FT /note="R -> H (found in a patient with primary ovarian
FT failure associated with intellectual disability and
FT sensorineural hearing loss; unknown pathological
FT significance; no change in glycosylation pattern;
FT dbSNP:rs143240087)"
FT /evidence="ECO:0000269|PubMed:27129271,
FT ECO:0000269|PubMed:30918116"
FT /id="VAR_083162"
FT VARIANT 272
FT /note="I -> V (no change in glycosylation pattern;
FT dbSNP:rs12793348)"
FT /evidence="ECO:0000269|PubMed:30918116"
FT /id="VAR_031225"
FT VARIANT 346
FT /note="K -> E (in OOMD7; impaired glycosylation resulting
FT in the absence of GLY2 and the accumulation of GLY1 forms;
FT associated with increased hemi-channel activity;
FT dbSNP:rs1591529130)"
FT /evidence="ECO:0000269|PubMed:30918116"
FT /id="VAR_083163"
FT VARIANT 347
FT /note="C -> S (in OOMD7; impaired glycosylation resulting
FT in the absence of GLY2 and the accumulation of GLY1 forms;
FT associated with increased hemichannel activity;
FT dbSNP:rs1212949833)"
FT /evidence="ECO:0000269|PubMed:20829356,
FT ECO:0000269|PubMed:30918116"
FT /id="VAR_083164"
FT VARIANT 392..426
FT /note="Missing (in OOMD7; impaired glycosylation resulting
FT in the absence of GLY2 and the accumulation of GLY1 forms;
FT associated with increased hemi-channel activity)"
FT /evidence="ECO:0000269|PubMed:30918116"
FT /id="VAR_083165"
FT MUTAGEN 255
FT /note="N->Q: Impaired glycosylation. Loss of GLY1 and GLY2
FT forms. No effect on oocyte survival."
FT /evidence="ECO:0000269|PubMed:17715132,
FT ECO:0000269|PubMed:30918116"
FT MUTAGEN 338
FT /note="N->Q: Impaired glycosylation; loss of GLY2 form;
FT oocyte death."
FT /evidence="ECO:0000269|PubMed:30918116"
FT MUTAGEN 394
FT /note="N->Q: No change in glycosylation pattern."
FT /evidence="ECO:0000269|PubMed:30918116"
FT CONFLICT 182..185
FT /note="Missing (in Ref. 7; AAK73361)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="D -> V (in Ref. 7; AAK73361)"
FT /evidence="ECO:0000305"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6M02"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 33..53
FT /evidence="ECO:0007829|PDB:6WBF"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7DWB"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6LTO"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6LTO"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 109..130
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 132..161
FT /evidence="ECO:0007829|PDB:6WBF"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:7DWB"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7DWB"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6M02"
FT HELIX 208..235
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:7F8N"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 270..295
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6WBN"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 327..338
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 343..354
FT /evidence="ECO:0007829|PDB:6WBF"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:6WBF"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:6WBF"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:7DWB"
FT TURN 384..395
FT /evidence="ECO:0007829|PDB:7DWB"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:7DWB"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6M02"
FT HELIX 415..421
FT /evidence="ECO:0007829|PDB:6M02"
SQ SEQUENCE 426 AA; 48050 MW; 368B48E0709424FB CRC64;
MAIAQLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KNSLQSESGN LPLWLHKFFP YILLLFAILL
YLPPLFWRFA AAPHICSDLK FIMEELDKVY NRAIKAAKSA RDLDMRDGAC SVPGVTENLG
QSLWEVSESH FKYPIVEQYL KTKKNSNNLI IKYISCRLLT LIIILLACIY LGYYFSLSSL
SDEFVCSIKS GILRNDSTVP DQFQCKLIAV GIFQLLSVIN LVVYVLLAPV VVYTLFVPFR
QKTDVLKVYE ILPTFDVLHF KSEGYNDLSL YNLFLEENIS EVKSYKCLKV LENIKSSGQG
IDPMLLLTNL GMIKMDVVDG KTPMSAEMRE EQGNQTAELQ GMNIDSETKA NNGEKNARQR
LLDSSC
