ID CCD47_HUMAN Reviewed; 483 AA. AC Q96A33; B2RAS8; D3DU20; Q96D00; Q96JZ7; Q9H3E4; Q9NRG3; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 28-JAN-2026, entry version 180. DE RecName: Full=PAT complex subunit CCDC47 {ECO:0000303|PubMed:32814900}; DE AltName: Full=Calumin {ECO:0000303|PubMed:25009997, ECO:0000303|PubMed:30401460}; DE AltName: Full=Coiled-coil domain-containing protein 47 {ECO:0000305}; DE Flags: Precursor; GN Name=CCDC47 {ECO:0000303|PubMed:30401460, GN ECO:0000312|HGNC:HGNC:24856}; ORFNames=GK001, MSTP041, PSEC0077; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver cancer; RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.; RT "A novel gene expressed in human liver cancer tissue."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, and Ovary; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-483 (ISOFORM 1). RC TISSUE=Heart; RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., RA Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25009997; DOI=10.1016/j.ydbio.2014.06.024; RA Yamamoto S., Yamazaki T., Komazaki S., Yamashita T., Osaki M., RA Matsubayashi M., Kidoya H., Takakura N., Yamazaki D., Kakizawa S.; RT "Contribution of calumin to embryogenesis through participation in the RT endoplasmic reticulum-associated degradation activity."; RL Dev. Biol. 393:33-43(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WDR83OS/ASTERIX. RX PubMed=32814900; DOI=10.1038/s41586-020-2624-y; RA Chitwood P.J., Hegde R.S.; RT "An intramembrane chaperone complex facilitates membrane protein RT biogenesis."; RL Nature 584:630-634(2020). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS) OF 52-239 IN COMPLEX WITH RP THE MULTI-PASS TRANSLOCON COMPLEX, FUNCTION, AND INTERACTION WITH TMCO1; RP TMEM147; NCLN; NOMO; SEC61A1; SEC61B AND SEC61G. RX PubMed=32820719; DOI=10.7554/elife.56889; RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J., RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.; RT "An ER translocon for multi-pass membrane protein biogenesis."; RL Elife 9:0-0(2020). RN [13] RP FUNCTION, IDENTIFICATION IN THE MULTI-PASS TRANSLOCON COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=36261522; DOI=10.1038/s41586-022-05330-8; RA Sundaram A., Yamsek M., Zhong F., Hooda Y., Hegde R.S., Keenan R.J.; RT "Substrate-driven assembly of a translocon for multipass membrane RT proteins."; RL Nature 611:167-172(2022). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN THNS, VARIANTS THNS RP 271-ARG--MET-483 DEL AND 397-ARG--MET-483 DEL, AND CHARACTERIZATION OF RP VARIANTS THNS 271-ARG--MET-483 DEL AND 397-ARG--MET-483 DEL. RX PubMed=30401460; DOI=10.1016/j.ajhg.2018.09.014; RA Morimoto M., Waller-Evans H., Ammous Z., Song X., Strauss K.A., RA Pehlivan D., Gonzaga-Jauregui C., Puffenberger E.G., Holst C.R., Karaca E., RA Brigatti K.W., Maguire E., Coban-Akdemir Z.H., Amagata A., Lau C.C., RA Chepa-Lotrea X., Macnamara E., Tos T., Isikay S., Nehrebecky M., RA Overton J.D., Klein M., Markello T.C., Posey J.E., Adams D.R., RA Lloyd-Evans E., Lupski J.R., Gahl W.A., Malicdan M.C.V.; RT "Bi-allelic CCDC47 variants cause a disorder characterized by woolly hair, RT liver dysfunction, dysmorphic features, and global developmental delay."; RL Am. J. Hum. Genet. 103:794-807(2018). CC -!- FUNCTION: Component of the multi-pass translocon (MPT) complex that CC mediates insertion of multi-pass membrane proteins into the lipid CC bilayer of membranes (PubMed:32814900, PubMed:32820719, CC PubMed:36261522). The MPT complex takes over after the SEC61 complex: CC following membrane insertion of the first few transmembrane segments of CC proteins by the SEC61 complex, the MPT complex occludes the lateral CC gate of the SEC61 complex to promote insertion of subsequent CC transmembrane regions (PubMed:36261522). Within the MPT complex, the CC PAT subcomplex sequesters any highly polar regions in the transmembrane CC domains away from the non-polar membrane environment until they can be CC buried in the interior of the fully assembled protein (By similarity). CC Within the PAT subcomplex, CCDC47 occludes the lateral gate of the CC SEC61 complex (By similarity). Involved in the regulation of calcium CC ion homeostasis in the ER (PubMed:30401460). Required for proper CC protein degradation via the ERAD (ER-associated degradation) pathway CC (PubMed:25009997). Has an essential role in the maintenance of ER CC organization during embryogenesis (By similarity). CC {ECO:0000250|UniProtKB:A0A8I3P7X4, ECO:0000250|UniProtKB:Q9D024, CC ECO:0000269|PubMed:25009997, ECO:0000269|PubMed:30401460, CC ECO:0000269|PubMed:32814900, ECO:0000269|PubMed:32820719, CC ECO:0000269|PubMed:36261522}. CC -!- SUBUNIT: Component of the PAT complex, composed of WDR83OS/Asterix and CC CCDC47 (PubMed:32814900, PubMed:36261522). The PAT complex is part of CC the multi-pass translocon (MPT) complex, composed of three CC subcomplexes, the GEL complex (composed of RAB5IF/OPTI and TMCO1), the CC BOS complex (composed of NCLN/Nicalin, NOMO and TMEM147) and the PAT CC complex (composed of WDR83OS/Asterix and CCDC47) (PubMed:32820719, CC PubMed:36261522). The MPT complex associates with the SEC61 complex CC (PubMed:32820719, PubMed:36261522). Interacts with VCP, HSPA5, DERL1, CC DERL2 and SELENOS (By similarity). {ECO:0000250|UniProtKB:Q9D024, CC ECO:0000269|PubMed:32814900, ECO:0000269|PubMed:32820719, CC ECO:0000269|PubMed:36261522}. CC -!- INTERACTION: CC Q96A33; Q92985: IRF7; NbExp=2; IntAct=EBI-720151, EBI-968267; CC Q96A33; Q92993: KAT5; NbExp=3; IntAct=EBI-720151, EBI-399080; CC Q96A33; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-720151, EBI-11742507; CC Q96A33; P17252: PRKCA; NbExp=3; IntAct=EBI-720151, EBI-1383528; CC Q96A33; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-720151, EBI-9090795; CC Q96A33; Q86WV6: STING1; NbExp=2; IntAct=EBI-720151, EBI-2800345; CC Q96A33; P58753: TIRAP; NbExp=2; IntAct=EBI-720151, EBI-528644; CC Q96A33; Q9Y284: WDR83OS; NbExp=3; IntAct=EBI-720151, EBI-6309120; CC Q96A33; P61981: YWHAG; NbExp=3; IntAct=EBI-720151, EBI-359832; CC Q96A33; Q99J34: Irak1; Xeno; NbExp=2; IntAct=EBI-720151, EBI-6117042; CC Q96A33; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-720151, EBI-6117196; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:25009997, ECO:0000269|PubMed:30401460, CC ECO:0000269|PubMed:32814900}; Single-pass type I membrane protein CC {ECO:0000255}. Rough endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9D024}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96A33-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96A33-2; Sequence=VSP_018478; CC -!- DISEASE: Trichohepatoneurodevelopmental syndrome (THNS) [MIM:618268]: CC An autosomal recessive complex multisystem disorder characterized by CC woolly or coarse hair, liver dysfunction, pruritus, dysmorphic CC features, hypotonia, and global developmental delay. CC {ECO:0000269|PubMed:30401460}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CCDC47 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG39292.1; Type=Frameshift; Evidence={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; AF226054; AAF86954.1; -; mRNA. DR EMBL; AK027786; BAB55367.1; -; mRNA. DR EMBL; AK027844; BAB55407.1; -; mRNA. DR EMBL; AK075387; BAC11587.1; -; mRNA. DR EMBL; AK314328; BAG36975.1; -; mRNA. DR EMBL; CH471109; EAW94279.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94281.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94282.1; -; Genomic_DNA. DR EMBL; BC008905; AAH08905.1; -; mRNA. DR EMBL; BC013600; AAH13600.2; -; mRNA. DR EMBL; AF113221; AAG39292.1; ALT_FRAME; mRNA. DR CCDS; CCDS11643.1; -. [Q96A33-1] DR RefSeq; NP_064583.2; NM_020198.3. [Q96A33-1] DR RefSeq; XP_005257584.1; XM_005257527.3. [Q96A33-1] DR RefSeq; XP_054172683.1; XM_054316708.1. [Q96A33-1] DR PDB; 6W6L; EM; 3.84 A; 7=1-483. DR PDBsum; 6W6L; -. DR AlphaFoldDB; Q96A33; -. DR SMR; Q96A33; -. DR BioGRID; 121318; 506. DR ComplexPortal; CPX-7020; PAT intramembrane chaperone complex. DR CORUM; Q96A33; -. DR FunCoup; Q96A33; 2382. DR IntAct; Q96A33; 341. DR MINT; Q96A33; -. DR STRING; 9606.ENSP00000225726; -. DR TCDB; 8.A.142.1.1; the pat intramembrane chaperone complex (pat) family. DR GlyCosmos; Q96A33; 1 site, No reported glycans. DR GlyGen; Q96A33; 4 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (3 sites). DR iPTMnet; Q96A33; -. DR MetOSite; Q96A33; -. DR PhosphoSitePlus; Q96A33; -. DR SwissPalm; Q96A33; -. DR BioMuta; CCDC47; -. DR DMDM; 74731083; -. DR jPOST; Q96A33; -. DR MassIVE; Q96A33; -. DR PaxDb; 9606-ENSP00000225726; -. DR PeptideAtlas; Q96A33; -. DR ProteomicsDB; 75902; -. [Q96A33-1] DR ProteomicsDB; 75903; -. [Q96A33-2] DR Pumba; Q96A33; -. DR Antibodypedia; 31338; 170 antibodies from 26 providers. DR DNASU; 57003; -. DR Ensembl; ENST00000225726.10; ENSP00000225726.5; ENSG00000108588.16. [Q96A33-1] DR Ensembl; ENST00000403162.7; ENSP00000384888.3; ENSG00000108588.16. [Q96A33-1] DR Ensembl; ENST00000582252.1; ENSP00000463577.1; ENSG00000108588.16. [Q96A33-2] DR GeneID; 57003; -. DR KEGG; hsa:57003; -. DR MANE-Select; ENST00000225726.10; ENSP00000225726.5; NM_020198.3; NP_064583.2. DR UCSC; uc002jbs.5; human. [Q96A33-1] DR AGR; HGNC:24856; -. DR ClinPGx; PA142672164; -. DR CTD; 57003; -. DR DisGeNET; 57003; -. DR GeneCards; CCDC47; -. DR HGNC; HGNC:24856; CCDC47. DR HPA; ENSG00000108588; Low tissue specificity. DR MalaCards; CCDC47; -. DR MIM; 618260; gene. DR MIM; 618268; phenotype. DR OpenTargets; ENSG00000108588; -. DR VEuPathDB; HostDB:ENSG00000108588; -. DR eggNOG; KOG2357; Eukaryota. DR GeneTree; ENSGT00390000013997; -. DR HOGENOM; CLU_033196_1_0_1; -. DR InParanoid; Q96A33; -. DR OMA; MHLVRDM; -. DR OrthoDB; 10039147at2759; -. DR PAN-GO; Q96A33; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q96A33; -. DR PathwayCommons; Q96A33; -. DR SignaLink; Q96A33; -. DR Agora; ENSG00000108588; -. DR BioGRID-ORCS; 57003; 53 hits in 1168 CRISPR screens. DR ChiTaRS; CCDC47; human. DR GenomeRNAi; 57003; -. DR Pharos; Q96A33; Tbio. DR PRO; PR:Q96A33; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96A33; protein. DR Bgee; ENSG00000108588; Expressed in calcaneal tendon and 196 other cell types or tissues. DR ExpressionAtlas; Q96A33; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0160064; C:multi-pass translocon complex; IDA:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; IPI:ComplexPortal. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IMP:UniProtKB. DR GO; GO:0006983; P:ER overload response; IEA:Ensembl. DR GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB. DR GO; GO:0160063; P:multi-pass transmembrane protein insertion into ER membrane; IDA:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:UniProtKB. DR InterPro; IPR012879; CCDC47. DR PANTHER; PTHR12883; ADIPOCYTE-SPECIFIC PROTEIN 4-RELATED; 1. DR PANTHER; PTHR12883:SF0; PAT COMPLEX SUBUNIT CCDC47; 1. DR Pfam; PF07946; CCDC47; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chaperone; Coiled coil; KW Disease variant; Endoplasmic reticulum; Glycoprotein; Membrane; KW Proteomics identification; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..483 FT /note="PAT complex subunit CCDC47" FT /id="PRO_0000235797" FT TOPO_DOM 21..135 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:A0A8I3P7X4" FT TRANSMEM 136..155 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 156..483 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:A0A8I3P7X4" FT REGION 46..118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 450..483 FT /evidence="ECO:0000255" FT COMPBIAS 60..104 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..118 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..472 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 473..483 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 178 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 458..483 FT /note="EAALRREQKKLEKKQMKMKQIKVKAM -> VRQTYHWGKTTICKDDCLCSVG FT C (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_018478" FT VARIANT 271..483 FT /note="Missing (in THNS; loss-of-function variant affecting FT ER calcium ion homeostasis in patient cells; no protein FT detected by Western blot in patient cells)" FT /evidence="ECO:0000269|PubMed:30401460" FT /id="VAR_081926" FT VARIANT 397..483 FT /note="Missing (in THNS; loss-of-function variant affecting FT ER calcium ion homeostasis in patient cells; no protein FT detected by Western blot in patient cells)" FT /evidence="ECO:0000269|PubMed:30401460" FT /id="VAR_081927" FT CONFLICT 464..465 FT /note="EQ -> AK (in Ref. 1; AAF86954)" FT /evidence="ECO:0000305" SQ SEQUENCE 483 AA; 55874 MW; 2C77CB7359B6A857 CRC64; MKAFHTFCVV LLVFGSVSEA KFDDFEDEED IVEYDDNDFA EFEDVMEDSV TESPQRVIIT EDDEDETTVE LEGQDENQEG DFEDADTQEG DTESEPYDDE EFEGYEDKPD TSSSKNKDPI TIVDVPAHLQ NSWESYYLEI LMVTGLLAYI MNYIIGKNKN SRLAQAWFNT HRELLESNFT LVGDDGTNKE ATSTGKLNQE NEHIYNLWCS GRVCCEGMLI QLRFLKRQDL LNVLARMMRP VSDQVQIKVT MNDEDMDTYV FAVGTRKALV RLQKEMQDLS EFCSDKPKSG AKYGLPDSLA ILSEMGEVTD GMMDTKMVHF LTHYADKIES VHFSDQFSGP KIMQEEGQPL KLPDTKRTLL FTFNVPGSGN TYPKDMEALL PLMNMVIYSI DKAKKFRLNR EGKQKADKNR ARVEENFLKL THVQRQEAAQ SRREEKKRAE KERIMNEEDP EKQRRLEEAA LRREQKKLEK KQMKMKQIKV KAM //