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 27-MAR-2024, entry version 218. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 1,4,5- RT 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 N- RT 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., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., 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., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., 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., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA 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., Haeseleer F., RA 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 BY RP 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., Buerckstuemmer T., RA 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 BY RP 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 VARIANT RP 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 and RT 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP INTERACTION WITH BCL2L10. RX PubMed=27995898; DOI=10.7554/elife.19896; RA Bonneau B., Ando H., Kawaai K., Hirose M., Takahashi-Iwanaga H., RA Mikoshiba K.; RT "IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, RT and by promoting ER-mitochondria contact."; RL Elife 5:e19896-e19896(2016). CC -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second messenger CC that mediates the release of intracellular calcium. This release is CC regulated by cAMP both dependently and independently of PKA (By CC similarity). {ECO:0000250|UniProtKB:Q9Z329}. CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with CABP1 CC (PubMed:12032348). Interacts with BOK; regulates ITPR2 expression (By CC similarity). Interacts with BCL2L10 (PubMed:27995898). Interacts with CC TRPC4 (By similarity). {ECO:0000250|UniProtKB:P29995, CC ECO:0000269|PubMed:12032348, ECO:0000269|PubMed:27995898}. 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 calcium CC 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, hair, CC nails, and skin are normal. {ECO:0000269|PubMed:25329695}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the CC receptor, most probably by interacting with a distinct calcium-binding CC protein which then inhibits the receptor. CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}. 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; 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 SMR; Q14571; -. DR BioGRID; 109914; 123. DR IntAct; Q14571; 32. DR MINT; Q14571; -. DR STRING; 9606.ENSP00000370744; -. DR BindingDB; Q14571; -. DR ChEMBL; CHEMBL2111451; -. DR DrugBank; DB00201; Caffeine. DR GlyCosmos; Q14571; 1 site, 1 glycan. DR GlyGen; Q14571; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q14571; -. DR MetOSite; Q14571; -. DR PhosphoSitePlus; Q14571; -. DR SwissPalm; Q14571; -. DR BioMuta; ITPR2; -. DR DMDM; 259016258; -. DR EPD; Q14571; -. DR jPOST; Q14571; -. DR MassIVE; Q14571; -. DR MaxQB; Q14571; -. DR PaxDb; 9606-ENSP00000370744; -. DR PeptideAtlas; Q14571; -. DR ProteomicsDB; 60049; -. [Q14571-1] DR ProteomicsDB; 60050; -. [Q14571-2] DR Pumba; Q14571; -. DR Antibodypedia; 24309; 155 antibodies from 31 providers. DR DNASU; 3709; -. DR Ensembl; ENST00000242737.5; ENSP00000242737.5; ENSG00000123104.12. [Q14571-2] DR Ensembl; ENST00000381340.8; ENSP00000370744.3; ENSG00000123104.12. [Q14571-1] DR GeneID; 3709; -. DR KEGG; hsa:3709; -. DR MANE-Select; ENST00000381340.8; ENSP00000370744.3; NM_002223.4; NP_002214.2. DR UCSC; uc001rhg.4; human. [Q14571-1] DR AGR; HGNC:6181; -. DR CTD; 3709; -. DR DisGeNET; 3709; -. DR GeneCards; ITPR2; -. DR HGNC; HGNC:6181; ITPR2. DR HPA; ENSG00000123104; Tissue enhanced (liver). 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 VEuPathDB; HostDB:ENSG00000123104; -. DR eggNOG; KOG3533; Eukaryota. DR GeneTree; ENSGT00940000156039; -. DR HOGENOM; CLU_000206_1_0_1; -. DR InParanoid; Q14571; -. DR OMA; PLETRAC; -. DR OrthoDB; 5480299at2759; -. DR PhylomeDB; Q14571; -. DR TreeFam; TF312815; -. DR PathwayCommons; Q14571; -. 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-9664323; FCGR3A-mediated IL10 synthesis. DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR SignaLink; Q14571; -. DR SIGNOR; Q14571; -. DR BioGRID-ORCS; 3709; 21 hits in 1151 CRISPR screens. DR ChiTaRS; ITPR2; human. DR GeneWiki; ITPR2; -. DR GenomeRNAi; 3709; -. DR Pharos; Q14571; Tbio. DR PRO; PR:Q14571; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q14571; Protein. DR Bgee; ENSG00000123104; Expressed in calcaneal tendon and 195 other cell types or tissues. DR ExpressionAtlas; Q14571; baseline and differential. DR GO; GO:0005938; C:cell cortex; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; 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:0044325; F:transmembrane transporter binding; IPI:ARUK-UCL. 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: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 Gene3D; 1.10.287.70; -; 1. DR Gene3D; 2.80.10.50; -; 2. DR Gene3D; 1.25.10.30; IP3 receptor type 1 binding core, RIH domain; 1. 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_IP3_receptor. DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf. DR PANTHER; PTHR45816:SF3; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; 1. DR PANTHER; PTHR45816; MIR DOMAIN-CONTAINING PROTEIN; 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; SSF48371; ARM repeat; 1. DR SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 2. DR SUPFAM; SSF82109; MIR domain; 2. DR PROSITE; PS50919; MIR; 5. DR Genevisible; Q14571; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Calcium channel; Calcium transport; KW Disease variant; Endoplasmic reticulum; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..2701 FT /note="Inositol 1,4,5-trisphosphate receptor type 2" FT /id="PRO_0000153924" FT TOPO_DOM 1..2227 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2228..2248 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2249..2260 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2261..2281 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2282..2307 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2308..2328 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2329..2351 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2352..2372 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2373..2394 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 2395..2415 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2416..2521 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2522..2542 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2543..2701 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 112..166 FT /note="MIR 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 173..223 FT /note="MIR 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 231..287 FT /note="MIR 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 294..372 FT /note="MIR 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 378..434 FT /note="MIR 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT REGION 1140..1174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1159..1174 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 265..269 FT /ligand="1D-myo-inositol 1,4,5-trisphosphate" FT /ligand_id="ChEBI:CHEBI:203600" FT /evidence="ECO:0000250" FT BINDING 507..510 FT /ligand="1D-myo-inositol 1,4,5-trisphosphate" FT /ligand_id="ChEBI:CHEBI:203600" FT /evidence="ECO:0000250" FT BINDING 567..569 FT /ligand="1D-myo-inositol 1,4,5-trisphosphate" FT /ligand_id="ChEBI:CHEBI:203600" FT /evidence="ECO:0000250" FT MOD_RES 937 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250|UniProtKB:Q9Z329" FT MOD_RES 1160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1709 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z329" FT MOD_RES 2607 FT /note="Phosphotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 2633 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z329" FT MOD_RES 2636 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z329" FT VAR_SEQ 176..181 FT /note="IVVGDK -> DASFWI (in isoform Short)" FT /evidence="ECO:0000303|PubMed:9729462" FT /id="VSP_002699" FT VAR_SEQ 182..2701 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:9729462" FT /id="VSP_002700" FT VARIANT 453 FT /note="A -> V (in dbSNP:rs2230384)" FT /id="VAR_055963" FT VARIANT 1143 FT /note="E -> D (in dbSNP:rs2230373)" FT /id="VAR_055964" FT VARIANT 1898 FT /note="A -> V (in dbSNP:rs2230382)" FT /id="VAR_055965" FT VARIANT 2498 FT /note="G -> S (in ANHD; loss of function mutation; FT dbSNP:rs786204832)" FT /evidence="ECO:0000269|PubMed:25329695" FT /id="VAR_073688" FT CONFLICT 597 FT /note="A -> P (in Ref. 1; BAA05384)" FT /evidence="ECO:0000305" FT CONFLICT 1070 FT /note="P -> A (in Ref. 1; BAA05384)" FT /evidence="ECO:0000305" FT CONFLICT 1178 FT /note="N -> K (in Ref. 1; BAA05384)" FT /evidence="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 //