GenomeNet

Database: UniProt
Entry: ITPR2_HUMAN
LinkDB: ITPR2_HUMAN
Original site: ITPR2_HUMAN 
ID   ITPR2_HUMAN             Reviewed;        2701 AA.
AC   Q14571; O94773;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   13-FEB-2019, entry version 189.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 2;
DE   AltName: Full=IP3 receptor isoform 2;
DE            Short=IP3R 2;
DE            Short=InsP3R2;
DE   AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 2 InsP3 receptor;
GN   Name=ITPR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX   PubMed=8081734;
RA   Yamamoto-Hino M., Sugiyama T., Hikiti K., Mattei M.-G., Hasegawa K.,
RA   Sekine S., Sakurada K., Miyawaki A., Furuichi T., Hasegawa M.,
RA   Mikoshiba K.;
RT   "Cloning and characterization of human type 2 and type 3 inositol
RT   1,4,5-trisphosphate receptors.";
RL   Recept. Channels 2:9-22(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   TISSUE=Heart;
RX   PubMed=9729462; DOI=10.1042/bj3340559;
RA   Futatsugi A., Kuwajima G., Mikoshiba K.;
RT   "Muscle-specific mRNA isoform encodes a protein composed mainly of the
RT   N-terminal 175 residues of type 2 Ins(1,4,5)P3 receptor.";
RL   Biochem. J. 334:559-563(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   INTERACTION WITH CABP1.
RX   PubMed=12032348; DOI=10.1073/pnas.102006299;
RA   Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K.,
RA   Haeseleer F., Foskett J.K.;
RT   "Identification of a family of calcium sensors as protein ligands of
RT   inositol trisphosphate receptor Ca(2+) release channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   INVOLVEMENT IN ANHD, VARIANT ANHD SER-2498, AND CHARACTERIZATION OF
RP   VARIANT ANHD SER-2498.
RX   PubMed=25329695; DOI=10.1172/JCI70720;
RA   Klar J., Hisatsune C., Baig S.M., Tariq M., Johansson A.C., Rasool M.,
RA   Malik N.A., Ameur A., Sugiura K., Feuk L., Mikoshiba K., Dahl N.;
RT   "Abolished InsP3R2 function inhibits sweat secretion in both humans
RT   and mice.";
RL   J. Clin. Invest. 124:4773-4780(2014).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second
CC       messenger that mediates the release of intracellular calcium. This
CC       release is regulated by cAMP both dependently and independently of
CC       PKA (By similarity). {ECO:0000250|UniProtKB:Q9Z329}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with CABP1
CC       (PubMed:12032348). Interacts with BOK; regulates ITPR2 expression
CC       (By similarity). {ECO:0000250|UniProtKB:P29995,
CC       ECO:0000269|PubMed:12032348}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q14571-1; Sequence=Displayed;
CC       Name=Short; Synonyms=TIPR;
CC         IsoId=Q14571-2; Sequence=VSP_002699, VSP_002700;
CC   -!- TISSUE SPECIFICITY: Isoform Short is found in skeletal muscle and
CC       heart.
CC   -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC       extremity. Its large N-terminal cytoplasmic region has the ligand-
CC       binding site in the N-terminus and modulatory sites in the middle
CC       portion immediately upstream of the channel region.
CC   -!- PTM: Phosphorylation by cAMP-dependent PKA on Ser-937 increases
CC       calcium release. {ECO:0000250}.
CC   -!- DISEASE: Anhidrosis, isolated, with normal sweat glands (ANHD)
CC       [MIM:106190]: An autosomal recessive disorder characterized by
CC       generalized, isolated anhidrosis, severe heat intolerance, and
CC       morphologically normal eccrine sweat glands. Body growth, teeth,
CC       hair, nails, and skin are normal. {ECO:0000269|PubMed:25329695}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the
CC       receptor, most probably by interacting with a distinct calcium-
CC       binding protein which then inhibits the receptor.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
DR   EMBL; D26350; BAA05384.1; -; mRNA.
DR   EMBL; AB012610; BAA33961.1; -; mRNA.
DR   EMBL; AC023051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC055720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS41764.1; -. [Q14571-1]
DR   RefSeq; NP_002214.2; NM_002223.3. [Q14571-1]
DR   UniGene; Hs.512235; -.
DR   ProteinModelPortal; Q14571; -.
DR   SMR; Q14571; -.
DR   BioGrid; 109914; 30.
DR   IntAct; Q14571; 10.
DR   MINT; Q14571; -.
DR   STRING; 9606.ENSP00000370744; -.
DR   ChEMBL; CHEMBL2111451; -.
DR   DrugBank; DB00201; Caffeine.
DR   iPTMnet; Q14571; -.
DR   PhosphoSitePlus; Q14571; -.
DR   BioMuta; ITPR2; -.
DR   DMDM; 259016258; -.
DR   EPD; Q14571; -.
DR   jPOST; Q14571; -.
DR   MaxQB; Q14571; -.
DR   PaxDb; Q14571; -.
DR   PeptideAtlas; Q14571; -.
DR   PRIDE; Q14571; -.
DR   ProteomicsDB; 60049; -.
DR   ProteomicsDB; 60050; -. [Q14571-2]
DR   Ensembl; ENST00000242737; ENSP00000242737; ENSG00000123104. [Q14571-2]
DR   Ensembl; ENST00000381340; ENSP00000370744; ENSG00000123104. [Q14571-1]
DR   GeneID; 3709; -.
DR   KEGG; hsa:3709; -.
DR   UCSC; uc001rhg.4; human. [Q14571-1]
DR   CTD; 3709; -.
DR   DisGeNET; 3709; -.
DR   EuPathDB; HostDB:ENSG00000123104.11; -.
DR   GeneCards; ITPR2; -.
DR   H-InvDB; HIX0036661; -.
DR   HGNC; HGNC:6181; ITPR2.
DR   HPA; HPA059144; -.
DR   HPA; HPA062260; -.
DR   MalaCards; ITPR2; -.
DR   MIM; 106190; phenotype.
DR   MIM; 600144; gene.
DR   neXtProt; NX_Q14571; -.
DR   OpenTargets; ENSG00000123104; -.
DR   Orphanet; 468666; Isolated generalized anhidrosis with normal sweat glands.
DR   PharmGKB; PA29979; -.
DR   eggNOG; KOG3533; Eukaryota.
DR   eggNOG; ENOG410XR97; LUCA.
DR   GeneTree; ENSGT00940000156039; -.
DR   HOGENOM; HOG000007660; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q14571; -.
DR   KO; K04959; -.
DR   OMA; ENQVKGG; -.
DR   OrthoDB; 94996at2759; -.
DR   PhylomeDB; Q14571; -.
DR   TreeFam; TF312815; -.
DR   Reactome; R-HSA-112043; PLC beta mediated events.
DR   Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-HSA-1489509; DAG and IP3 signaling.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-HSA-4086398; Ca2+ pathway.
DR   Reactome; R-HSA-422356; Regulation of insulin secretion.
DR   Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   Reactome; R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   ChiTaRS; ITPR2; human.
DR   GeneWiki; ITPR2; -.
DR   GenomeRNAi; 3709; -.
DR   PRO; PR:Q14571; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000123104; Expressed in 219 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q14571; baseline and differential.
DR   Genevisible; Q14571; HS.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IMP:BHF-UCL.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:BHF-UCL.
DR   GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR000699; RIH_dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR   PANTHER; PTHR13715; PTHR13715; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 4.
DR   SUPFAM; SSF100909; SSF100909; 2.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Complete proteome; Disease mutation; Endoplasmic reticulum;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2701       Inositol 1,4,5-trisphosphate receptor
FT                                type 2.
FT                                /FTId=PRO_0000153924.
FT   TOPO_DOM      1   2227       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2228   2248       Helical. {ECO:0000255}.
FT   TOPO_DOM   2249   2260       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2261   2281       Helical. {ECO:0000255}.
FT   TOPO_DOM   2282   2307       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2308   2328       Helical. {ECO:0000255}.
FT   TOPO_DOM   2329   2351       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2352   2372       Helical. {ECO:0000255}.
FT   TOPO_DOM   2373   2394       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   2395   2415       Helical. {ECO:0000255}.
FT   TOPO_DOM   2416   2521       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2522   2542       Helical. {ECO:0000255}.
FT   TOPO_DOM   2543   2701       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      112    166       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      173    223       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      231    287       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      294    372       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      378    434       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   REGION      265    269       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      507    510       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   REGION      567    569       Inositol 1,4,5-trisphosphate binding.
FT                                {ECO:0000250}.
FT   MOD_RES     937    937       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    1160   1160       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1709   1709       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2607   2607       Phosphotyrosine. {ECO:0000255}.
FT   MOD_RES    2633   2633       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   MOD_RES    2636   2636       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z329}.
FT   VAR_SEQ     176    181       IVVGDK -> DASFWI (in isoform Short).
FT                                {ECO:0000303|PubMed:9729462}.
FT                                /FTId=VSP_002699.
FT   VAR_SEQ     182   2701       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:9729462}.
FT                                /FTId=VSP_002700.
FT   VARIANT     453    453       A -> V (in dbSNP:rs2230384).
FT                                /FTId=VAR_055963.
FT   VARIANT    1143   1143       E -> D (in dbSNP:rs2230373).
FT                                /FTId=VAR_055964.
FT   VARIANT    1898   1898       A -> V (in dbSNP:rs2230382).
FT                                /FTId=VAR_055965.
FT   VARIANT    2498   2498       G -> S (in ANHD; loss of function
FT                                mutation; dbSNP:rs786204832).
FT                                {ECO:0000269|PubMed:25329695}.
FT                                /FTId=VAR_073688.
FT   CONFLICT    597    597       A -> P (in Ref. 1; BAA05384).
FT                                {ECO:0000305}.
FT   CONFLICT   1070   1070       P -> A (in Ref. 1; BAA05384).
FT                                {ECO:0000305}.
FT   CONFLICT   1178   1178       N -> K (in Ref. 1; BAA05384).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2701 AA;  308064 MW;  373BA20228A159BC CRC64;
     MTEKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
     CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENKKL LGEIVKYSNV
     IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
     KVVLMPVNAG QPLHASNIEL LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV
     RLFHAEQEKF LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
     SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGVPPTS KKKRQAGEKI MYTLVSVPHG
     NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTDEE RPVMLKIGTC
     QTKEDKEAFA IVSVPLSEVR DLDFANDANK VLATTVKKLE NGTITQNERR FVTKLLEDLI
     FFVADVPNNG QEVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
     LGDQRYAPYK YMLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NTTAIPVTQE LICKFMLSPG
     NADILIQTKV VSMQADNPME SSILSDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAKEGT
     KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR
     LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
     YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
     SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MSVPDVPPSI HPSKQGSPTE
     HEDVTVMDTK LKIIEILQFI LSVRLDYRIS YMLSIYKKEF GEDNDNAETS ASGSPDTLLP
     SAIVPDIDEI AAQAETMFAG RKEKNPVQLD DEGGRTFLRV LIHLIMHDYP PLLSGALQLL
     FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSSNYENGE
     IGESQVKGGE EPIEESNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR
     NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP QNQVLLHKHL
     NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
     GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLHMMC SERDRGDESG PLAYHITLVE
     LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
     IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADIFLEKCVT ESIMNIVSGF FNSPFSDNST
     SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA IPVDLDSQVN
     TLFMKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEHQFSPM
     MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
     MLEKKDSFVE EGNTLRKILL NRYFKGDYSI GVNGHLSGAY SKTAQVGGSF SGQDSDKMGI
     SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGIFLGIA LLEGGNTQTQ YSFYQQLHEQ
     KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD NELMTSGPRM RVRDSTLHLK
     EGMKGQLTEA SSATSKAYCV YRREMDPEID IMCTGPEAGN TEEKSAEEVT MSPAIAIMQP
     ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK
     NVALVNQNLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
     KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDGVS
     PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDEGDEALK YYANHTAQIE IVRHDRTMEQ
     IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF
     WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PLFSVLLWIA VAICTSMLFF
     FSKPVGIRPF LVSIMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
     ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
     LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGSHQV PTMTLTTMME ACAKENCSPT
     IPASNTADEE YEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
     DLLFYFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE
     EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMIVE KNLDWFPRMR AMSLVSNEGD
     SEQNEIRSLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP
     H
//
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