CCD47_HUMAN
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 03-AUG-2022, entry version 163.
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;
DE Flags: Precursor;
GN Name=CCDC47 {ECO:0000312|HGNC:HGNC:24856};
GN 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 FUNCTION, AND INTERACTION WITH TMCO1; TMEM147; NCLN; NOMO; SEC61A1; SEC61B
RP 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, 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 PAT complex, an endoplasmic reticulum (ER)-
CC resident membrane multiprotein complex that facilitates multi-pass
CC membrane proteins insertion into membranes (PubMed:32814900). The PAT
CC complex acts as an intramembrane chaperone by directly interacting with
CC nascent transmembrane domains (TMDs), releasing its substrates upon
CC correct folding, and is needed for optimal biogenesis of multi-pass
CC membrane proteins (PubMed:32814900). WDR83OS/Asterix is the substrate-
CC interacting subunit of the PAT complex, whereas CCDC47 is required to
CC maintain the stability of WDR83OS/Asterix (PubMed:32814900). The PAT
CC complex favors the binding to TMDs with exposed hydrophilic amino acids
CC within the lipid bilayer and provides a membrane-embedded partially
CC hydrophilic environment in which the first transmembrane domain binds
CC (PubMed:32814900). Component of a ribosome-associated ER translocon
CC complex involved in multi-pass membrane protein transport into the ER
CC membrane and biogenesis (PubMed:32820719). Involved in the regulation
CC of calcium ion homeostasis in the ER (PubMed:30401460). Required for
CC proper protein degradation via the ERAD (ER-associated degradation)
CC pathway (PubMed:25009997). Has an essential role in the maintenance of
CC ER organization during embryogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9D024, ECO:0000269|PubMed:25009997,
CC ECO:0000269|PubMed:30401460, ECO:0000269|PubMed:32814900,
CC ECO:0000269|PubMed:32820719}.
CC -!- SUBUNIT: The PAT complex includes WDR83OS/Asterix and CCDC47
CC (PubMed:32814900). The ribosome-associated ER translocon complex
CC includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and
CC TMEM147; in the absence of ribosomes, only the complex forms with
CC NCLN/Nicalin, NOMO and TMEM147 remains intact (PubMed:32820719).
CC Interacts with VCP, HSPA5, DERL1, DERL2 and SELENOS (By similarity).
CC {ECO:0000250|UniProtKB:Q9D024, ECO:0000269|PubMed:32814900,
CC ECO:0000269|PubMed:32820719}.
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=2; 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 membrane protein
CC {ECO:0000305}. Rough endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9D024}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG39292.1; Type=Frameshift; Evidence={ECO:0000305};
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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_020198.2. [Q96A33-1]
DR RefSeq; XP_005257584.1; XM_005257527.2. [Q96A33-1]
DR PDB; 6W6L; EM; 3.84 A; 7=1-483.
DR PDBsum; 6W6L; -.
DR AlphaFoldDB; Q96A33; -.
DR SMR; Q96A33; -.
DR BioGRID; 121318; 251.
DR ComplexPortal; CPX-7020; PAT intramembrane chaperone complex.
DR IntAct; Q96A33; 74.
DR MINT; Q96A33; -.
DR STRING; 9606.ENSP00000225726; -.
DR TCDB; 8.A.142.1.1; the pat intramembrane chaperone complex (pat) family.
DR GlyGen; Q96A33; 1 site.
DR iPTMnet; Q96A33; -.
DR MetOSite; Q96A33; -.
DR PhosphoSitePlus; Q96A33; -.
DR SwissPalm; Q96A33; -.
DR BioMuta; CCDC47; -.
DR DMDM; 74731083; -.
DR EPD; Q96A33; -.
DR jPOST; Q96A33; -.
DR MassIVE; Q96A33; -.
DR MaxQB; Q96A33; -.
DR PaxDb; Q96A33; -.
DR PeptideAtlas; Q96A33; -.
DR PRIDE; Q96A33; -.
DR ProteomicsDB; 75902; -. [Q96A33-1]
DR ProteomicsDB; 75903; -. [Q96A33-2]
DR Antibodypedia; 31338; 176 antibodies from 24 providers.
DR DNASU; 57003; -.
DR Ensembl; ENST00000225726.10; ENSP00000225726.5; ENSG00000108588.15. [Q96A33-1]
DR Ensembl; ENST00000403162.7; ENSP00000384888.3; ENSG00000108588.15. [Q96A33-1]
DR Ensembl; ENST00000582252.1; ENSP00000463577.1; ENSG00000108588.15. [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 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 neXtProt; NX_Q96A33; -.
DR OpenTargets; ENSG00000108588; -.
DR PharmGKB; PA142672164; -.
DR VEuPathDB; HostDB:ENSG00000108588; -.
DR eggNOG; KOG2357; Eukaryota.
DR GeneTree; ENSGT00390000013997; -.
DR HOGENOM; CLU_033196_1_0_1; -.
DR InParanoid; Q96A33; -.
DR OMA; PPIDQKV; -.
DR OrthoDB; 1337297at2759; -.
DR PhylomeDB; Q96A33; -.
DR TreeFam; TF314902; -.
DR PathwayCommons; Q96A33; -.
DR SignaLink; Q96A33; -.
DR BioGRID-ORCS; 57003; 43 hits in 1090 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 194 other tissues.
DR ExpressionAtlas; Q96A33; baseline and differential.
DR Genevisible; Q96A33; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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: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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR InterPro; IPR012879; CCDC47.
DR PANTHER; PTHR12883; PTHR12883; 1.
DR Pfam; PF07946; DUF1682; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Coiled coil;
KW Disease variant; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; 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 TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000255"
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 63..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..471
FT /note="Basic and acidic 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
