ASPH_HUMAN
ID ASPH_HUMAN Reviewed; 758 AA.
AC Q12797; A0A0A0MSK8; A6NDF4; A6NHI2; B4DIC9; B4E2K4; B7ZM95; E5RGP5; F5H667;
AC Q6NXR7; Q8TB28; Q9H291; Q9H2C4; Q9NRI0; Q9NRI1; Q9Y4J0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Aspartyl/asparaginyl beta-hydroxylase;
DE EC=1.14.11.16 {ECO:0000269|PubMed:11773073};
DE AltName: Full=Aspartate beta-hydroxylase;
DE Short=ASP beta-hydroxylase;
DE AltName: Full=Peptide-aspartate beta-dioxygenase;
GN Name=ASPH; Synonyms=BAH;
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 1).
RX PubMed=7821814; DOI=10.1016/0378-1119(94)90460-x;
RA Korioth F., Gieffers C., Frey J.;
RT "Cloning and characterization of the human gene encoding aspartyl beta-
RT hydroxylase.";
RL Gene 150:395-399(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8823296; DOI=10.1172/jci118918;
RA Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M.,
RA Wands J.R., Friedman P.A.;
RT "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in
RT hepatocellular carcinoma and cholangiocarcinoma.";
RL J. Clin. Invest. 98:1313-1323(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Heart;
RX PubMed=10974562; DOI=10.1016/s0378-1119(00)00299-7;
RA Lim K.Y., Hong C.-S., Kim D.H.;
RT "cDNA cloning and characterization of human cardiac junctin.";
RL Gene 255:35-42(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=10956665; DOI=10.1074/jbc.m006753200;
RA Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J.,
RA O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F.,
RA Friedman P.A.;
RT "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform
RT of Asph missing the catalytic domain share exons with junctin.";
RL J. Biol. Chem. 275:39543-39554(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), CALCIUM-BINDING, ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Muscle;
RX PubMed=11007777; DOI=10.1074/jbc.m005473200;
RA Treves S., Feriotto G., Moccagatta L., Gambari R., Zorzato F.;
RT "Molecular cloning, expression, functional characterization, chromosomal
RT localization, and gene structure of junctate, a novel integral calcium
RT binding protein of sarco(endo)plasmic reticulum membrane.";
RL J. Biol. Chem. 275:39555-39568(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Heart;
RX PubMed=10767180; DOI=10.1006/mgme.2000.2966;
RA Wetzel G.T., Ding S., Chen F.;
RT "Molecular cloning of junctin from human and developing rabbit heart.";
RL Mol. Genet. Metab. 69:252-258(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 9 AND 10).
RC TISSUE=Hippocampus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7).
RC TISSUE=Brain, and Pancreatic carcinoma;
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP FUNCTION, CALCIUM-BINDING DOMAIN, INTERACTION WITH ORAI1 AND STIM1 (ISOFORM
RP 8), MUTAGENESIS OF 91-ASP--ASP-93, AND SUBCELLULAR LOCATION.
RX PubMed=22586105; DOI=10.1073/pnas.1200667109;
RA Srikanth S., Jew M., Kim K.D., Yee M.K., Abramson J., Gwack Y.;
RT "Junctate is a Ca2+-sensing structural component of Orai1 and stromal
RT interaction molecule 1 (STIM1).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:8682-8687(2012).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-452, AND GLYCOSYLATION [LARGE
RP SCALE ANALYSIS] AT ASN-64 (ISOFORM 3).
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP INTERACTION WITH CASQ2 (ISOFORM 4), AND SUBCELLULAR LOCATION.
RX PubMed=15485681; DOI=10.1016/j.cardiores.2004.09.009;
RA Houle T.D., Ram M.L., Cala S.E.;
RT "Calsequestrin mutant D307H exhibits depressed binding to its protein
RT targets and a depressed response to calcium.";
RL Cardiovasc. Res. 64:227-233(2004).
RN [16]
RP FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY.
RX PubMed=11773073; DOI=10.1074/jbc.m110389200;
RA Dinchuk J.E., Focht R.J., Kelley J.A., Henderson N.L., Zolotarjova N.I.,
RA Wynn R., Neff N.T., Link J., Huber R.M., Burn T.C., Rupar M.J.,
RA Cunningham M.R., Selling B.H., Ma J., Stern A.A., Hollis G.F., Stein R.B.,
RA Friedman P.A.;
RT "Absence of post-translational aspartyl beta-hydroxylation of epidermal
RT growth factor domains in mice leads to developmental defects and an
RT increased incidence of intestinal neoplasia.";
RL J. Biol. Chem. 277:12970-12977(2002).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP 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 [18]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 562-758 IN COMPLEX WITH
RP N-OXALYOLGLYCINE AND ZINC IONS, AND DISULFIDE BOND.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human aspartate beta-hydroxylase isoform A.";
RL Submitted (MAY-2011) to the PDB data bank.
RN [19]
RP INVOLVEMENT IN FDLAB, AND VARIANT FDLAB TRP-735.
RX PubMed=24768550; DOI=10.1016/j.ajhg.2014.04.002;
RA Patel N., Khan A.O., Mansour A., Mohamed J.Y., Al-Assiri A., Haddad R.,
RA Jia X., Xiong Y., Megarbane A., Traboulsi E.I., Alkuraya F.S.;
RT "Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-
RT segment abnormalities, and spontaneous filtering blebs, or Traboulsi
RT syndrome.";
RL Am. J. Hum. Genet. 94:755-759(2014).
CC -!- FUNCTION: [Isoform 1]: Specifically hydroxylates an Asp or Asn residue
CC in certain epidermal growth factor-like (EGF) domains of a number of
CC proteins. {ECO:0000269|PubMed:11773073}.
CC -!- FUNCTION: [Isoform 8]: Membrane-bound Ca(2+)-sensing protein, which is
CC a structural component of the ER-plasma membrane junctions. Isoform 8
CC regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC)
CC channels in T-cells. {ECO:0000269|PubMed:22586105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartyl-[protein] + O2 = 3-hydroxy-L-
CC aspartyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:11508,
CC Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:14951, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17427,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:30031; EC=1.14.11.16;
CC Evidence={ECO:0000269|PubMed:11773073};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q28056};
CC -!- SUBUNIT: Monomer (By similarity). Isoform 8 interacts with ORAI1 and
CC STIM1. Isoform 4 interacts with CASQ2. {ECO:0000250|UniProtKB:Q28056,
CC ECO:0000269|PubMed:15485681, ECO:0000269|PubMed:22586105}.
CC -!- INTERACTION:
CC Q12797; O43681: GET3; NbExp=3; IntAct=EBI-2967294, EBI-2515857;
CC Q12797-6; O95994: AGR2; NbExp=3; IntAct=EBI-12092171, EBI-712648;
CC Q12797-6; P02818: BGLAP; NbExp=3; IntAct=EBI-12092171, EBI-12927282;
CC Q12797-6; P01037: CST1; NbExp=3; IntAct=EBI-12092171, EBI-1056240;
CC Q12797-6; Q5JRM2: CXorf66; NbExp=3; IntAct=EBI-12092171, EBI-12823659;
CC Q12797-6; P81605: DCD; NbExp=3; IntAct=EBI-12092171, EBI-395625;
CC Q12797-6; P60022: DEFB1; NbExp=3; IntAct=EBI-12092171, EBI-7200390;
CC Q12797-6; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-12092171, EBI-3923585;
CC Q12797-6; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-12092171, EBI-356015;
CC Q12797-6; Q6UWR7: ENPP6; NbExp=3; IntAct=EBI-12092171, EBI-13382816;
CC Q12797-6; Q8NFU4: FDCSP; NbExp=3; IntAct=EBI-12092171, EBI-12210457;
CC Q12797-6; Q14512: FGFBP1; NbExp=3; IntAct=EBI-12092171, EBI-953742;
CC Q12797-6; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12092171, EBI-3918971;
CC Q12797-6; P22466: GAL; NbExp=3; IntAct=EBI-12092171, EBI-6624768;
CC Q12797-6; P01350: GAST; NbExp=3; IntAct=EBI-12092171, EBI-3436637;
CC Q12797-6; O43681: GET3; NbExp=3; IntAct=EBI-12092171, EBI-2515857;
CC Q12797-6; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-12092171, EBI-712073;
CC Q12797-6; Q8TDV5: GPR119; NbExp=3; IntAct=EBI-12092171, EBI-17253531;
CC Q12797-6; Q96SL4: GPX7; NbExp=3; IntAct=EBI-12092171, EBI-749411;
CC Q12797-6; Q8TED1: GPX8; NbExp=3; IntAct=EBI-12092171, EBI-11721746;
CC Q12797-6; O15499: GSC2; NbExp=3; IntAct=EBI-12092171, EBI-19954058;
CC Q12797-6; Q02747: GUCA2A; NbExp=3; IntAct=EBI-12092171, EBI-12244272;
CC Q12797-6; P42858: HTT; NbExp=6; IntAct=EBI-12092171, EBI-466029;
CC Q12797-6; Q9HBE4: IL21; NbExp=3; IntAct=EBI-12092171, EBI-6595560;
CC Q12797-6; Q9Y5Q6: INSL5; NbExp=3; IntAct=EBI-12092171, EBI-21626318;
CC Q12797-6; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-12092171, EBI-22452746;
CC Q12797-6; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-12092171, EBI-751501;
CC Q12797-6; Q6PIL6: KCNIP4; NbExp=3; IntAct=EBI-12092171, EBI-1051469;
CC Q12797-6; Q92876: KLK6; NbExp=3; IntAct=EBI-12092171, EBI-2432309;
CC Q12797-6; P80188: LCN2; NbExp=3; IntAct=EBI-12092171, EBI-11911016;
CC Q12797-6; P30533: LRPAP1; NbExp=3; IntAct=EBI-12092171, EBI-715927;
CC Q12797-6; P01374: LTA; NbExp=3; IntAct=EBI-12092171, EBI-524105;
CC Q12797-6; Q9NX40: OCIAD1; NbExp=3; IntAct=EBI-12092171, EBI-2683029;
CC Q12797-6; Q6UW60: PCSK4; NbExp=3; IntAct=EBI-12092171, EBI-13342757;
CC Q12797-6; P04085-2: PDGFA; NbExp=5; IntAct=EBI-12092171, EBI-11995148;
CC Q12797-6; Q9NWW9: PLAAT2; NbExp=3; IntAct=EBI-12092171, EBI-12253270;
CC Q12797-6; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12092171, EBI-742388;
CC Q12797-6; Q59EV6: PPGB; NbExp=3; IntAct=EBI-12092171, EBI-14210385;
CC Q12797-6; Q96NZ9: PRAP1; NbExp=3; IntAct=EBI-12092171, EBI-2116102;
CC Q12797-6; A5D903: PRB1; NbExp=6; IntAct=EBI-12092171, EBI-10173935;
CC Q12797-6; P02812: PRB2; NbExp=3; IntAct=EBI-12092171, EBI-19951389;
CC Q12797-6; P01270: PTH; NbExp=3; IntAct=EBI-12092171, EBI-716817;
CC Q12797-6; P21246: PTN; NbExp=3; IntAct=EBI-12092171, EBI-473725;
CC Q12797-6; Q15293: RCN1; NbExp=3; IntAct=EBI-12092171, EBI-948278;
CC Q12797-6; Q8NC24: RELL2; NbExp=3; IntAct=EBI-12092171, EBI-10269209;
CC Q12797-6; O60930: RNASEH1; NbExp=3; IntAct=EBI-12092171, EBI-2372399;
CC Q12797-6; P0DMR2: SCGB1C2; NbExp=3; IntAct=EBI-12092171, EBI-12947705;
CC Q12797-6; P34741: SDC2; NbExp=5; IntAct=EBI-12092171, EBI-1172957;
CC Q12797-6; Q15428: SF3A2; NbExp=3; IntAct=EBI-12092171, EBI-2462271;
CC Q12797-6; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-12092171, EBI-744081;
CC Q12797-6; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-12092171, EBI-18037857;
CC Q12797-6; Q86UW2: SLC51B; NbExp=5; IntAct=EBI-12092171, EBI-12266756;
CC Q12797-6; P58511: SMIM11; NbExp=3; IntAct=EBI-12092171, EBI-1051936;
CC Q12797-6; Q96E16: SMIM19; NbExp=3; IntAct=EBI-12092171, EBI-17657124;
CC Q12797-6; P08294: SOD3; NbExp=3; IntAct=EBI-12092171, EBI-10195782;
CC Q12797-6; P00995: SPINK1; NbExp=3; IntAct=EBI-12092171, EBI-8054204;
CC Q12797-6; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-12092171, EBI-17684533;
CC Q12797-6; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12092171, EBI-6447886;
CC Q12797-6; O14763: TNFRSF10B; NbExp=3; IntAct=EBI-12092171, EBI-518882;
CC Q12797-6; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-12092171, EBI-12261790;
CC Q12797-6; Q96J42: TXNDC15; NbExp=3; IntAct=EBI-12092171, EBI-2908241;
CC Q12797-6; O75310: UGT2B11; NbExp=3; IntAct=EBI-12092171, EBI-12891746;
CC Q12797-6; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-12092171, EBI-11958577;
CC Q12797-6; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-12092171, EBI-12175871;
CC Q12797-6; O60844: ZG16; NbExp=3; IntAct=EBI-12092171, EBI-746479;
CC Q12797-6; A0A087WZY1; NbExp=3; IntAct=EBI-12092171, EBI-13387614;
CC Q12797-6; A0A1U9X8X8; NbExp=3; IntAct=EBI-12092171, EBI-17234977;
CC Q12797-7; P42858: HTT; NbExp=3; IntAct=EBI-25953099, EBI-466029;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane;
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Sarcoplasmic reticulum membrane;
CC Single-pass type II membrane protein {ECO:0000305|PubMed:15485681}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Endoplasmic reticulum membrane;
CC Single-pass type II membrane protein {ECO:0000269|PubMed:22586105}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Comment: 3 functionally distinct proteins are produced by
CC alternative splicing: Aspartyl/asparaginyl beta-hydroxylase, Junctin
CC and Junctate. Additional isoforms are produced by alternative
CC splicing. {ECO:0000269|PubMed:11007777};
CC Name=1;
CC IsoId=Q12797-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12797-2; Sequence=VSP_039169, VSP_039170;
CC Name=3; Synonyms=Junctin-1, Cardiac junctin;
CC IsoId=Q12797-3; Sequence=VSP_039165, VSP_039166, VSP_039167,
CC VSP_039168;
CC Name=4; Synonyms=Junctin-2, Junctin;
CC IsoId=Q12797-4; Sequence=VSP_039165, VSP_039167, VSP_039168;
CC Name=5;
CC IsoId=Q12797-5; Sequence=VSP_039165, VSP_039166, VSP_044238,
CC VSP_039169, VSP_039170;
CC Name=10;
CC IsoId=Q12797-10; Sequence=VSP_039165;
CC Name=6;
CC IsoId=Q12797-6; Sequence=VSP_044236, VSP_039169, VSP_039170;
CC Name=7;
CC IsoId=Q12797-7; Sequence=VSP_039166, VSP_044235, VSP_044237;
CC Name=8; Synonyms=Junctate;
CC IsoId=Q12797-8; Sequence=VSP_039165, VSP_039166, VSP_039169,
CC VSP_039170;
CC Name=9;
CC IsoId=Q12797-9; Sequence=VSP_039165, VSP_039166, VSP_044236,
CC VSP_039169, VSP_039170;
CC Name=11;
CC IsoId=Q12797-11; Sequence=VSP_059345, VSP_039169, VSP_039170;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in all tissues tested.
CC Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and
CC liver. Isoform 8 is expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:11007777}.
CC -!- DISEASE: Facial dysmorphism, lens dislocation, anterior segment
CC abnormalities, and spontaneous filtering blebs (FDLAB) [MIM:601552]: A
CC syndrome characterized by dislocated crystalline lenses and anterior
CC segment abnormalities in association with a distinctive facies
CC involving flat cheeks and a beaked nose. Some affected individuals
CC develop highly unusual non-traumatic conjunctival cysts (filtering
CC blebs). {ECO:0000269|PubMed:24768550}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000305}.
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DR EMBL; U03109; AAA82108.1; -; mRNA.
DR EMBL; S83325; AAB50779.1; -; mRNA.
DR EMBL; AF224468; AAF82246.1; -; mRNA.
DR EMBL; AF224469; AAF82247.1; -; mRNA.
DR EMBL; AF289489; AAG40811.1; -; mRNA.
DR EMBL; AF306765; AAG42257.1; -; mRNA.
DR EMBL; AF184241; AAG16983.1; -; mRNA.
DR EMBL; AK295528; BAG58441.1; -; mRNA.
DR EMBL; AK304314; BAG65166.1; -; mRNA.
DR EMBL; AC067881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471068; EAW86841.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86840.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86847.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86848.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86849.1; -; Genomic_DNA.
DR EMBL; BC025236; AAH25236.1; -; mRNA.
DR EMBL; BC066929; AAH66929.1; -; mRNA.
DR EMBL; BC142967; AAI42968.1; -; mRNA.
DR EMBL; BC144362; AAI44363.1; -; mRNA.
DR CCDS; CCDS34898.1; -. [Q12797-1]
DR CCDS; CCDS34899.1; -. [Q12797-4]
DR CCDS; CCDS34900.1; -. [Q12797-3]
DR CCDS; CCDS43742.1; -. [Q12797-2]
DR CCDS; CCDS47866.1; -. [Q12797-8]
DR CCDS; CCDS55234.1; -. [Q12797-10]
DR CCDS; CCDS55235.1; -. [Q12797-9]
DR CCDS; CCDS55236.1; -. [Q12797-5]
DR CCDS; CCDS55237.1; -. [Q12797-6]
DR CCDS; CCDS55238.1; -. [Q12797-7]
DR CCDS; CCDS75746.1; -. [Q12797-11]
DR PIR; I38423; I38423.
DR RefSeq; NP_001158222.1; NM_001164750.1. [Q12797-10]
DR RefSeq; NP_001158223.1; NM_001164751.1. [Q12797-5]
DR RefSeq; NP_001158225.1; NM_001164753.1. [Q12797-9]
DR RefSeq; NP_001158227.1; NM_001164755.1. [Q12797-6]
DR RefSeq; NP_001158228.1; NM_001164756.1. [Q12797-7]
DR RefSeq; NP_004309.2; NM_004318.3. [Q12797-1]
DR RefSeq; NP_064549.1; NM_020164.4. [Q12797-3]
DR RefSeq; NP_115855.1; NM_032466.3. [Q12797-2]
DR RefSeq; NP_115856.1; NM_032467.3. [Q12797-4]
DR RefSeq; NP_115857.1; NM_032468.4. [Q12797-8]
DR PDB; 5APA; X-ray; 2.05 A; A=562-758.
DR PDB; 5JQY; X-ray; 1.99 A; A=330-758.
DR PDB; 5JTC; X-ray; 2.24 A; A=330-758.
DR PDB; 5JZ6; X-ray; 2.35 A; A=330-758.
DR PDB; 5JZ8; X-ray; 2.10 A; A=330-758.
DR PDB; 5JZA; X-ray; 2.14 A; A=330-758.
DR PDB; 5JZU; X-ray; 2.50 A; A=330-758.
DR PDB; 6Q9F; X-ray; 1.63 A; A=330-758.
DR PDB; 6Q9I; X-ray; 1.85 A; A=330-758.
DR PDB; 6QA5; X-ray; 2.65 A; A=330-758.
DR PDB; 6RK9; X-ray; 2.29 A; A/B=330-758.
DR PDB; 6YYU; X-ray; 2.11 A; A=330-758.
DR PDB; 6YYV; X-ray; 1.77 A; A=330-758.
DR PDB; 6YYW; X-ray; 2.27 A; A=330-758.
DR PDB; 6YYX; X-ray; 1.53 A; A=330-758.
DR PDB; 6YYY; X-ray; 2.29 A; A=330-758.
DR PDB; 6Z6Q; X-ray; 1.81 A; A=330-758.
DR PDB; 6Z6R; X-ray; 2.13 A; A=330-758.
DR PDB; 7BMI; X-ray; 1.66 A; A=330-758.
DR PDB; 7BMJ; X-ray; 1.75 A; A/C=330-758.
DR PDB; 7E6J; X-ray; 1.90 A; A=330-758.
DR PDBsum; 5APA; -.
DR PDBsum; 5JQY; -.
DR PDBsum; 5JTC; -.
DR PDBsum; 5JZ6; -.
DR PDBsum; 5JZ8; -.
DR PDBsum; 5JZA; -.
DR PDBsum; 5JZU; -.
DR PDBsum; 6Q9F; -.
DR PDBsum; 6Q9I; -.
DR PDBsum; 6QA5; -.
DR PDBsum; 6RK9; -.
DR PDBsum; 6YYU; -.
DR PDBsum; 6YYV; -.
DR PDBsum; 6YYW; -.
DR PDBsum; 6YYX; -.
DR PDBsum; 6YYY; -.
DR PDBsum; 6Z6Q; -.
DR PDBsum; 6Z6R; -.
DR PDBsum; 7BMI; -.
DR PDBsum; 7BMJ; -.
DR PDBsum; 7E6J; -.
DR AlphaFoldDB; Q12797; -.
DR SMR; Q12797; -.
DR BioGRID; 106936; 296.
DR IntAct; Q12797; 143.
DR MINT; Q12797; -.
DR STRING; 9606.ENSP00000368767; -.
DR BindingDB; Q12797; -.
DR ChEMBL; CHEMBL4680030; -.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB00139; Succinic acid.
DR DrugCentral; Q12797; -.
DR TCDB; 8.A.28.1.5; the ankyrin (ankyrin) family.
DR GlyConnect; 1018; 13 N-Linked glycans (1 site).
DR GlyGen; Q12797; 7 sites, 13 N-linked glycans (1 site), 4 O-linked glycans (4 sites).
DR iPTMnet; Q12797; -.
DR PhosphoSitePlus; Q12797; -.
DR SwissPalm; Q12797; -.
DR BioMuta; ASPH; -.
DR DMDM; 145559444; -.
DR EPD; Q12797; -.
DR jPOST; Q12797; -.
DR MassIVE; Q12797; -.
DR MaxQB; Q12797; -.
DR PaxDb; Q12797; -.
DR PeptideAtlas; Q12797; -.
DR PRIDE; Q12797; -.
DR ProteomicsDB; 27096; -.
DR ProteomicsDB; 4295; -.
DR ProteomicsDB; 58944; -. [Q12797-1]
DR ProteomicsDB; 58945; -. [Q12797-2]
DR ProteomicsDB; 58946; -. [Q12797-3]
DR ProteomicsDB; 58947; -. [Q12797-4]
DR ProteomicsDB; 66767; -.
DR ProteomicsDB; 7252; -.
DR ProteomicsDB; 73953; -.
DR ProteomicsDB; 80510; -.
DR TopDownProteomics; Q12797-1; -. [Q12797-1]
DR TopDownProteomics; Q12797-2; -. [Q12797-2]
DR Antibodypedia; 24707; 325 antibodies from 30 providers.
DR DNASU; 444; -.
DR Ensembl; ENST00000356457.9; ENSP00000348841.5; ENSG00000198363.18. [Q12797-2]
DR Ensembl; ENST00000379449.10; ENSP00000368762.5; ENSG00000198363.18. [Q12797-7]
DR Ensembl; ENST00000379454.9; ENSP00000368767.4; ENSG00000198363.18. [Q12797-1]
DR Ensembl; ENST00000389204.8; ENSP00000373856.4; ENSG00000198363.18. [Q12797-3]
DR Ensembl; ENST00000445642.6; ENSP00000394013.4; ENSG00000198363.18. [Q12797-11]
DR Ensembl; ENST00000517847.6; ENSP00000429954.2; ENSG00000198363.18. [Q12797-8]
DR Ensembl; ENST00000517903.5; ENSP00000430245.1; ENSG00000198363.18. [Q12797-5]
DR Ensembl; ENST00000518068.5; ENSP00000429286.1; ENSG00000198363.18. [Q12797-6]
DR Ensembl; ENST00000522603.5; ENSP00000436188.1; ENSG00000198363.18. [Q12797-4]
DR Ensembl; ENST00000522835.5; ENSP00000429160.1; ENSG00000198363.18. [Q12797-9]
DR Ensembl; ENST00000541428.5; ENSP00000437864.1; ENSG00000198363.18. [Q12797-10]
DR GeneID; 444; -.
DR KEGG; hsa:444; -.
DR MANE-Select; ENST00000379454.9; ENSP00000368767.4; NM_004318.4; NP_004309.2.
DR UCSC; uc003xuj.4; human. [Q12797-1]
DR CTD; 444; -.
DR DisGeNET; 444; -.
DR GeneCards; ASPH; -.
DR HGNC; HGNC:757; ASPH.
DR HPA; ENSG00000198363; Tissue enhanced (adipose).
DR MalaCards; ASPH; -.
DR MIM; 600582; gene.
DR MIM; 601552; phenotype.
DR neXtProt; NX_Q12797; -.
DR OpenTargets; ENSG00000198363; -.
DR Orphanet; 412022; Facial dysmorphism-lens dislocation-anterior segment abnormalities-spontaneous filtering blebs syndrome.
DR PharmGKB; PA25056; -.
DR VEuPathDB; HostDB:ENSG00000198363; -.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000156304; -.
DR HOGENOM; CLU_106984_0_0_1; -.
DR InParanoid; Q12797; -.
DR OMA; YTELVKX; -.
DR OrthoDB; 1511606at2759; -.
DR PhylomeDB; Q12797; -.
DR TreeFam; TF312799; -.
DR BRENDA; 1.14.11.16; 2681.
DR PathwayCommons; Q12797; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR SignaLink; Q12797; -.
DR BioGRID-ORCS; 444; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; ASPH; human.
DR EvolutionaryTrace; Q12797; -.
DR GeneWiki; ASPH; -.
DR GenomeRNAi; 444; -.
DR Pharos; Q12797; Tbio.
DR PRO; PR:Q12797; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q12797; protein.
DR Bgee; ENSG00000198363; Expressed in calcaneal tendon and 200 other tissues.
DR ExpressionAtlas; Q12797; baseline and differential.
DR Genevisible; Q12797; HS.
DR GO; GO:0034704; C:calcium channel complex; TAS:BHF-UCL.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; TAS:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; TAS:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; TAS:ProtInc.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0044325; F:transmembrane transporter binding; TAS:BHF-UCL.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0032237; P:activation of store-operated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0055074; P:calcium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0005513; P:detection of calcium ion; TAS:BHF-UCL.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0035108; P:limb morphogenesis; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IBA:GO_Central.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
DR GO; GO:0010649; P:regulation of cell communication by electrical coupling; TAS:BHF-UCL.
DR GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:1901879; P:regulation of protein depolymerization; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; TAS:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; IDA:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR039038; ASPH.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12366; PTHR12366; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Dioxygenase; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Signal-anchor; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..758
FT /note="Aspartyl/asparaginyl beta-hydroxylase"
FT /id="PRO_0000064706"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..758
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 341..374
FT /note="TPR 1"
FT REPEAT 454..487
FT /note="TPR 2"
FT REPEAT 489..521
FT /note="TPR 3"
FT REPEAT 525..557
FT /note="TPR 4"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:22586105"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:22586105"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:22586105"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:22586105"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:22586105"
FT BINDING 625
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|Ref.18"
FT BINDING 668
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|Ref.18"
FT BINDING 679
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 688..690
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|Ref.18"
FT BINDING 725
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305"
FT BINDING 735
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|Ref.18"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 641..648
FT /evidence="ECO:0000269|Ref.18"
FT VAR_SEQ 1..34
FT /note="MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARR -> MAEDK (in
FT isoform 3, isoform 4, isoform 5, isoform 8, isoform 9 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:10767180,
FT ECO:0000303|PubMed:10974562, ECO:0000303|PubMed:11007777,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_039165"
FT VAR_SEQ 84
FT /note="L -> LAKAKDFRYNLSEVLQ (in isoform 3, isoform 5,
FT isoform 7, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:10767180,
FT ECO:0000303|PubMed:10974562, ECO:0000303|PubMed:11007777,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_039166"
FT VAR_SEQ 108..239
FT /note="GLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMV
FT HAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETV
FT SQDCNQDMEEMMSEQENPDSS -> EGPSGVAKRKTKAKVKELTKEELKKEKEKPESRK
FT ESKNEERKKGKKEDVRKDKKIADADLSRKESPKGKKDREKEKVDLEKSAKTKENRKKST
FT NMKDVSSKMASRDKDDRKESRSSTRYAHLTKGNTQKRNG (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10767180,
FT ECO:0000303|PubMed:10974562"
FT /id="VSP_039167"
FT VAR_SEQ 110..188
FT /note="KERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHA
FT EHVEGEDLQQEDGPTGEPQQEDDEFLM -> TKDGSNENIDSLEEVLNILAEESSDWFY
FT GFLSFLYDIMTPFEMLEEEEEESETADGVDGTSQNEGVQGKTCVILDLHNQ (in
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044235"
FT VAR_SEQ 164..206
FT /note="Missing (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_044236"
FT VAR_SEQ 189..758
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044237"
FT VAR_SEQ 218..236
FT /note="Missing (in isoform 11)"
FT /id="VSP_059345"
FT VAR_SEQ 240..758
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10767180,
FT ECO:0000303|PubMed:10974562"
FT /id="VSP_039168"
FT VAR_SEQ 264
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044238"
FT VAR_SEQ 312..313
FT /note="ET -> DT (in isoform 2, isoform 5, isoform 6,
FT isoform 8, isoform 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10956665,
FT ECO:0000303|PubMed:11007777, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039169"
FT VAR_SEQ 314..758
FT /note="Missing (in isoform 2, isoform 5, isoform 6, isoform
FT 8, isoform 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10956665,
FT ECO:0000303|PubMed:11007777, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039170"
FT VARIANT 354
FT /note="R -> M (in dbSNP:rs6995412)"
FT /id="VAR_053781"
FT VARIANT 735
FT /note="R -> W (in FDLAB; dbSNP:rs374385878)"
FT /evidence="ECO:0000269|PubMed:24768550"
FT /id="VAR_071821"
FT MUTAGEN 91..93
FT /note="DAD->AAA: Increase in cytoplasmic Ca(2+) via
FT activation of endogenous CRAC channels."
FT /evidence="ECO:0000269|PubMed:22586105"
FT CONFLICT 519
FT /note="D -> N (in Ref. 7; BAG65166)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="Y -> I (in Ref. 1; AAA82108)"
FT /evidence="ECO:0000305"
FT CONFLICT 575..577
FT /note="WWT -> CG (in Ref. 1; AAA82108)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="E -> Q (in Ref. 1; AAA82108)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="D -> Y (in Ref. 7; BAG65166)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="K -> R (in Ref. 2; AAB50779)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="F -> L (in Ref. 7; BAG65166)"
FT /evidence="ECO:0000305"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 375..392
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6Q9F"
FT HELIX 416..432
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 436..449
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 454..466
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 470..483
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 488..500
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 525..538
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 543..552
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 584..592
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 594..607
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:6YYX"
FT TURN 617..619
FT /evidence="ECO:0007829|PDB:6YYV"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 625..632
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 638..643
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 645..651
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 686..694
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 697..704
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 725..729
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:6YYX"
FT STRAND 735..743
FT /evidence="ECO:0007829|PDB:6YYX"
FT HELIX 749..754
FT /evidence="ECO:0007829|PDB:6YYX"
FT CARBOHYD Q12797-3:64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 85863 MW; 4AE56D1D8DF0AF0C CRC64;
MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS GTSFFTWFMV
IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV DDAKVLLGLK ERSTSEPAVP
PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ
QEDDEFLMAT DVDDRFETLE PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE
PVVEDERLHH DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI
FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK LRKRGKIEEA
VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG AIETYQEVAS LPDVPADLLK
LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV
LSVTPNDGFA KVHYGFILKA QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN
KEAYKWYELG HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE
GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL LEKFPETTGC
RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC KIRCANETKT WEEGKVLIFD
DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ QRRSLPAI
