CLPB_HUMAN
ID CLPB_HUMAN Reviewed; 707 AA.
AC Q9H078; B4DXJ7; B4DXP7; B4DXW4; E7EWN6; F8W7P6; Q8ND11; Q9H8Y0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Caseinolytic peptidase B protein homolog;
DE EC=3.6.1.- {ECO:0000269|PubMed:25597510};
DE AltName: Full=Suppressor of potassium transport defect 3;
DE Flags: Precursor;
GN Name=CLPB; Synonyms=HSP78, SKD3;
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=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-589, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 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 [8]
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 [9]
RP INTERACTION WITH AKAP1; ATAD3A; MAVS; PHB AND PHB2, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=31522117; DOI=10.1016/j.isci.2019.08.056;
RA Yoshinaka T., Kosako H., Yoshizumi T., Furukawa R., Hirano Y., Kuge O.,
RA Tamada T., Koshiba T.;
RT "Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes:
RT Insight into a Role of the Coiled-Coil Region.";
RL IScience 19:1065-1078(2019).
RN [10]
RP VARIANTS MGCA7 CYS-272; GLY-408; ILE-411; 435-ASP-PRO-436 DELINS ASP-PRO;
RP ARG-486; LYS-501; CYS-567; VAL-591; CYS-617; VAL-646 AND ASN-682, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25597510; DOI=10.1016/j.ajhg.2014.12.013;
RA Wortmann S.B., Zietkiewicz S., Kousi M., Szklarczyk R., Haack T.B.,
RA Gersting S.W., Muntau A.C., Rakovic A., Renkema G.H., Rodenburg R.J.,
RA Strom T.M., Meitinger T., Rubio-Gozalbo M.E., Chrusciel E., Distelmaier F.,
RA Golzio C., Jansen J.H., van Karnebeek C., Lillquist Y., Luecke T.,
RA Ounap K., Zordania R., Yaplito-Lee J., van Bokhoven H., Spelbrink J.N.,
RA Vaz F.M., Pras-Raves M., Ploski R., Pronicka E., Klein C., Willemsen M.A.,
RA de Brouwer A.P., Prokisch H., Katsanis N., Wevers R.A.;
RT "CLPB mutations cause 3-methylglutaconic aciduria, progressive brain
RT atrophy, intellectual disability, congenital neutropenia, cataracts,
RT movement disorder.";
RL Am. J. Hum. Genet. 96:245-257(2015).
RN [11]
RP VARIANT MGCA7 MET-268, AND TISSUE SPECIFICITY.
RX PubMed=25597511; DOI=10.1016/j.ajhg.2014.12.020;
RA Saunders C., Smith L., Wibrand F., Ravn K., Bross P., Thiffault I.,
RA Christensen M., Atherton A., Farrow E., Miller N., Kingsmore S.F.,
RA Ostergaard E.;
RT "CLPB variants associated with autosomal-recessive mitochondrial disorder
RT with cataract, neutropenia, epilepsy, and methylglutaconic aciduria.";
RL Am. J. Hum. Genet. 96:258-265(2015).
CC -!- FUNCTION: May function as a regulatory ATPase and be related to
CC secretion/protein trafficking process. Involved in mitochondrial-
CC mediated antiviral innate immunity, activates RIG-I-mediated signal
CC transduction and production of IFNB1 and pro-inflammatory cytokine IL6
CC (PubMed:31522117). {ECO:0000269|PubMed:31522117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:25597510};
CC -!- SUBUNIT: Interacts with PHB and PHB2 (PubMed:31522117). Interacts with
CC MAVS; the interaction is enhanced by Sendai virus infection
CC (PubMed:31522117). {ECO:0000269|PubMed:31522117}.
CC -!- INTERACTION:
CC Q9H078; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2107221, EBI-739624;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:25597510, ECO:0000269|PubMed:31522117}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H078-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H078-2; Sequence=VSP_001106;
CC Name=3;
CC IsoId=Q9H078-3; Sequence=VSP_044726, VSP_001106;
CC Name=4;
CC IsoId=Q9H078-4; Sequence=VSP_044725;
CC Name=5;
CC IsoId=Q9H078-5; Sequence=VSP_057397, VSP_001106;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level)
CC (PubMed:25597511). Expressed in fetal, as well as in adult tissues,
CC with highest levels in adult brain, including thalamus, hippocampus,
CC occipital cortex and parietal cortex. Low expression in granulocytes
CC (PubMed:25597510). {ECO:0000269|PubMed:25597510,
CC ECO:0000269|PubMed:25597511}.
CC -!- DISEASE: 3-methylglutaconic aciduria 7 (MGCA7) [MIM:616271]: An
CC autosomal recessive inborn error of metabolism with a highly variable
CC phenotype. Primary disease symptoms are increased levels of 3-
CC methylglutaconic acid, neurologic deterioration and neutropenia. Other
CC common features include progressive encephalopathy, movement
CC abnormalities, delayed psychomotor development, cataracts, seizures,
CC and recurrent infections. {ECO:0000269|PubMed:25597510,
CC ECO:0000269|PubMed:25597511}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AL136909; CAB66843.1; -; mRNA.
DR EMBL; AL834484; CAD39142.1; -; mRNA.
DR EMBL; AK023214; BAB14467.1; -; mRNA.
DR EMBL; AK302006; BAG63409.1; -; mRNA.
DR EMBL; AK302069; BAG63459.1; -; mRNA.
DR EMBL; AK302158; BAG63526.1; -; mRNA.
DR EMBL; AP000593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006404; AAH06404.1; -; mRNA.
DR CCDS; CCDS58152.1; -. [Q9H078-4]
DR CCDS; CCDS58153.1; -. [Q9H078-3]
DR CCDS; CCDS58154.1; -. [Q9H078-2]
DR CCDS; CCDS8215.1; -. [Q9H078-1]
DR RefSeq; NP_001245321.1; NM_001258392.2. [Q9H078-2]
DR RefSeq; NP_001245322.1; NM_001258393.2. [Q9H078-3]
DR RefSeq; NP_001245323.1; NM_001258394.2. [Q9H078-4]
DR RefSeq; NP_110440.1; NM_030813.5. [Q9H078-1]
DR AlphaFoldDB; Q9H078; -.
DR SMR; Q9H078; -.
DR BioGRID; 123531; 199.
DR IntAct; Q9H078; 88.
DR MINT; Q9H078; -.
DR STRING; 9606.ENSP00000294053; -.
DR GlyGen; Q9H078; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H078; -.
DR MetOSite; Q9H078; -.
DR PhosphoSitePlus; Q9H078; -.
DR SwissPalm; Q9H078; -.
DR BioMuta; CLPB; -.
DR DMDM; 25009267; -.
DR EPD; Q9H078; -.
DR jPOST; Q9H078; -.
DR MassIVE; Q9H078; -.
DR MaxQB; Q9H078; -.
DR PaxDb; Q9H078; -.
DR PeptideAtlas; Q9H078; -.
DR PRIDE; Q9H078; -.
DR ProteomicsDB; 18882; -.
DR ProteomicsDB; 29984; -.
DR ProteomicsDB; 5473; -.
DR ProteomicsDB; 80212; -. [Q9H078-1]
DR ProteomicsDB; 80213; -. [Q9H078-2]
DR Antibodypedia; 30838; 198 antibodies from 27 providers.
DR DNASU; 81570; -.
DR Ensembl; ENST00000294053.9; ENSP00000294053.3; ENSG00000162129.14. [Q9H078-1]
DR Ensembl; ENST00000340729.9; ENSP00000340385.5; ENSG00000162129.14. [Q9H078-3]
DR Ensembl; ENST00000437826.6; ENSP00000407296.2; ENSG00000162129.14. [Q9H078-4]
DR Ensembl; ENST00000538039.6; ENSP00000441518.1; ENSG00000162129.14. [Q9H078-2]
DR GeneID; 81570; -.
DR KEGG; hsa:81570; -.
DR MANE-Select; ENST00000538039.6; ENSP00000441518.1; NM_001258392.3; NP_001245321.1. [Q9H078-2]
DR UCSC; uc001osj.5; human. [Q9H078-1]
DR UCSC; uc010rqz.3; human.
DR CTD; 81570; -.
DR DisGeNET; 81570; -.
DR GeneCards; CLPB; -.
DR GeneReviews; CLPB; -.
DR HGNC; HGNC:30664; CLPB.
DR HPA; ENSG00000162129; Tissue enriched (testis).
DR MalaCards; CLPB; -.
DR MIM; 616254; gene.
DR MIM; 616271; phenotype.
DR neXtProt; NX_Q9H078; -.
DR OpenTargets; ENSG00000162129; -.
DR Orphanet; 445038; 3-methylglutaconic aciduria type 7.
DR Orphanet; 486; Autosomal dominant severe congenital neutropenia.
DR PharmGKB; PA142672092; -.
DR VEuPathDB; HostDB:ENSG00000162129; -.
DR eggNOG; KOG1051; Eukaryota.
DR GeneTree; ENSGT00390000012961; -.
DR HOGENOM; CLU_005070_9_3_1; -.
DR InParanoid; Q9H078; -.
DR OMA; CKNAIFI; -.
DR PhylomeDB; Q9H078; -.
DR TreeFam; TF328654; -.
DR PathwayCommons; Q9H078; -.
DR SignaLink; Q9H078; -.
DR BioGRID-ORCS; 81570; 101 hits in 1082 CRISPR screens.
DR ChiTaRS; CLPB; human.
DR GeneWiki; CLPB; -.
DR GenomeRNAi; 81570; -.
DR Pharos; Q9H078; Tbio.
DR PRO; PR:Q9H078; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H078; protein.
DR Bgee; ENSG00000162129; Expressed in sperm and 121 other tissues.
DR ExpressionAtlas; Q9H078; baseline and differential.
DR Genevisible; Q9H078; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0039529; P:RIG-I signaling pathway; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; ATP-binding; Cataract;
KW Disease variant; Epilepsy; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..707
FT /note="Caseinolytic peptidase B protein homolog"
FT /id="PRO_0000191239"
FT REPEAT 133..162
FT /note="ANK 1"
FT REPEAT 166..195
FT /note="ANK 2"
FT REPEAT 265..295
FT /note="ANK 3"
FT REPEAT 298..327
FT /note="ANK 4"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 589
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057397"
FT VAR_SEQ 1..151
FT /note="MLGSLVLRRKALAPRLLLRLLRSPTLRGHGGASGRNVTTGSLGEPQWLRVAT
FT GGRPGTSPALFSGRGAATGGRQGGRFDTKCLAAATWGRLPGPEETLPGQDSWNGVPSRA
FT GLGMCALAAALVVHCYSKSPSNKDAALLEAARANNMQEVS -> MPRGCHLGTPSWSRR
FT NTPRTGQLERGPQQGRTGHVRPGRSAGGSLLQQESVQQGCSPVGSCPCQQYARSQQPQE
FT TAKNDAQSRSWAGLNAGVSLKNTKISSSEWPL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044725"
FT VAR_SEQ 152..180
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044726"
FT VAR_SEQ 216..245
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001106"
FT VARIANT 268
FT /note="T -> M (in MGCA7; dbSNP:rs200032855)"
FT /evidence="ECO:0000269|PubMed:25597511"
FT /id="VAR_073397"
FT VARIANT 272
FT /note="Y -> C (in MGCA7; dbSNP:rs777313457)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073398"
FT VARIANT 295
FT /note="R -> T (in dbSNP:rs7938203)"
FT /id="VAR_048740"
FT VARIANT 408
FT /note="R -> G (in MGCA7; reduced ATPase activity in vitro;
FT dbSNP:rs144078282)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073399"
FT VARIANT 411
FT /note="M -> I (in MGCA7; dbSNP:rs786205137)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073400"
FT VARIANT 435..436
FT /note="EG -> DP (in MGCA7)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073401"
FT VARIANT 486
FT /note="C -> R (in MGCA7; dbSNP:rs886041118)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073402"
FT VARIANT 501
FT /note="E -> K (in MGCA7; dbSNP:rs748915609)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073403"
FT VARIANT 567
FT /note="Y -> C (in MGCA7; dbSNP:rs150857620)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073404"
FT VARIANT 591
FT /note="A -> V (in MGCA7; dbSNP:rs748010262)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073405"
FT VARIANT 617
FT /note="Y -> C (in MGCA7; dbSNP:rs786205138)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073406"
FT VARIANT 646
FT /note="G -> V (in MGCA7; dbSNP:rs759500860)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073407"
FT VARIANT 682
FT /note="I -> N (in MGCA7; dbSNP:rs886041120)"
FT /evidence="ECO:0000269|PubMed:25597510"
FT /id="VAR_073408"
FT CONFLICT 413
FT /note="E -> K (in Ref. 2; BAG63459)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="N -> S (in Ref. 2; BAG63409)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="R -> C (in Ref. 2; BAG63459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78729 MW; 0E0F2A244CA20635 CRC64;
MLGSLVLRRK ALAPRLLLRL LRSPTLRGHG GASGRNVTTG SLGEPQWLRV ATGGRPGTSP
ALFSGRGAAT GGRQGGRFDT KCLAAATWGR LPGPEETLPG QDSWNGVPSR AGLGMCALAA
ALVVHCYSKS PSNKDAALLE AARANNMQEV SRLLSEGADV NAKHRLGWTA LMVAAINRNN
SVVQVLLAAG ADPNLGDDFS SVYKTAKEQG IHSLEDGGQD GASRHITNQW TSALEFRRWL
GLPAGVLITR EDDFNNRLNN RASFKGCTAL HYAVLADDYR TVKELLDGGA NPLQRNEMGH
TPLDYAREGE VMKLLRTSEA KYQEKQRKRE AEERRRFPLE QRLKEHIIGQ ESAIATVGAA
IRRKENGWYD EEHPLVFLFL GSSGIGKTEL AKQTAKYMHK DAKKGFIRLD MSEFQERHEV
AKFIGSPPGY VGHEEGGQLT KKLKQCPNAV VLFDEVDKAH PDVLTIMLQL FDEGRLTDGK
GKTIDCKDAI FIMTSNVASD EIAQHALQLR QEALEMSRNR IAENLGDVQI SDKITISKNF
KENVIRPILK AHFRRDEFLG RINEIVYFLP FCHSELIQLV NKELNFWAKR AKQRHNITLL
WDREVADVLV DGYNVHYGAR SIKHEVERRV VNQLAAAYEQ DLLPGGCTLR ITVEDSDKQL
LKSPELPSPQ AEKRLPKLRL EIIDKDSKTR RLDIRAPLHP EKVCNTI
