TTC7A_HUMAN
ID TTC7A_HUMAN Reviewed; 858 AA.
AC Q9ULT0; Q2T9J9; Q6PIX4; Q8ND67; Q9BUS3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Tetratricopeptide repeat protein 7A {ECO:0000305};
DE Short=TPR repeat protein 7A {ECO:0000305};
GN Name=TTC7A {ECO:0000312|HGNC:HGNC:19750};
GN Synonyms=KIAA1140 {ECO:0000303|PubMed:10574461}, TTC7;
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), AND VARIANT LEU-538.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-858 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 409-858 (ISOFORM 1).
RC TISSUE=Cervix, and Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-647, AND
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 [11]
RP FUNCTION.
RX PubMed=23229899; DOI=10.1083/jcb.201206095;
RA Nakatsu F., Baskin J.M., Chung J., Tanner L.B., Shui G., Lee S.Y.,
RA Pirruccello M., Hao M., Ingolia N.T., Wenk M.R., De Camilli P.;
RT "PtdIns4P synthesis by PI4KIIIalpha at the plasma membrane and its impact
RT on plasma membrane identity.";
RL J. Cell Biol. 199:1003-1016(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-182; SER-647; SER-690
RP AND THR-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647 AND THR-693, AND
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 [14]
RP INVOLVEMENT IN GIDID1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25546680; DOI=10.1097/md.0000000000000327;
RA Fernandez I., Patey N., Marchand V., Birlea M., Maranda B., Haddad E.,
RA Decaluwe H., Le Deist F.;
RT "Multiple intestinal atresia with combined immune deficiency related to
RT TTC7A defect is a multiorgan pathology: study of a French-Canadian-based
RT cohort.";
RL Medicine (Baltimore) 93:E327-E327(2014).
RN [15]
RP INTERACTION WITH PI4KA.
RX PubMed=34415310; DOI=10.1093/brain/awab313;
RA Salter C.G., Cai Y., Lo B., Helman G., Taylor H., McCartney A.,
RA Leslie J.S., Accogli A., Zara F., Traverso M., Fasham J., Lees J.A.,
RA Ferla M.P., Chioza B.A., Wenger O., Scott E., Cross H.E., Crawford J.,
RA Warshawsky I., Keisling M., Agamanolis D., Ward Melver C., Cox H.,
RA Elawad M., Marton T., Wakeling M.N., Holzinger D., Tippelt S., Munteanu M.,
RA Valcheva D., Deal C., Van Meerbeke S., Walsh Vockley C., Butte M.J.,
RA Acar U., van der Knaap M.S., Korenke G.C., Kotzaeridou U., Balla T.,
RA Simons C., Uhlig H.H., Crosby A.H., De Camilli P., Wolf N.I., Baple E.L.;
RT "Biallelic PI4KA variants cause neurological, intestinal and immunological
RT disease.";
RL Brain 144:3597-3610(2021).
RN [16]
RP VARIANTS GIDID1 PRO-399; ARG-606; PRO-672; SER-678 DEL; GLN-712 DEL AND
RP PRO-823.
RX PubMed=23830146; DOI=10.1016/j.jaci.2013.06.013;
RA Chen R., Giliani S., Lanzi G., Mias G.I., Lonardi S., Dobbs K., Manis J.,
RA Im H., Gallagher J.E., Phanstiel D.H., Euskirchen G., Lacroute P.,
RA Bettinger K., Moratto D., Weinacht K., Montin D., Gallo E., Mangili G.,
RA Porta F., Notarangelo L.D., Pedretti S., Al-Herz W., Alfahdli W.,
RA Comeau A.M., Traister R.S., Pai S.Y., Carella G., Facchetti F.,
RA Nadeau K.C., Snyder M., Notarangelo L.D.;
RT "Whole-exome sequencing identifies tetratricopeptide repeat domain 7A
RT (TTC7A) mutations for combined immunodeficiency with intestinal atresias.";
RL J. Allergy Clin. Immunol. 132:656-664(2013).
RN [17]
RP VARIANT GIDID1 PRO-823.
RX PubMed=23423984; DOI=10.1136/jmedgenet-2012-101483;
RA Samuels M.E., Majewski J., Alirezaie N., Fernandez I., Casals F., Patey N.,
RA Decaluwe H., Gosselin I., Haddad E., Hodgkinson A., Idaghdour Y.,
RA Marchand V., Michaud J.L., Rodrigue M.A., Desjardins S., Dubois S.,
RA Le Deist F., Awadalla P., Raymond V., Maranda B.;
RT "Exome sequencing identifies mutations in the gene TTC7A in French-Canadian
RT cases with hereditary multiple intestinal atresia.";
RL J. Med. Genet. 50:324-329(2013).
RN [18]
RP VARIANTS GIDID1 LYS-71; GLN-526 DEL AND THR-832, CHARACTERIZATION OF
RP VARIANTS GIDID1 LYS-71 AND THR-832, FUNCTION, AND INTERACTION WITH PI4KA.
RX PubMed=24417819; DOI=10.1053/j.gastro.2014.01.015;
RA Avitzur Y., Guo C., Mastropaolo L.A., Bahrami E., Chen H., Zhao Z.,
RA Elkadri A., Dhillon S., Murchie R., Fattouh R., Huynh H., Walker J.L.,
RA Wales P.W., Cutz E., Kakuta Y., Dudley J., Kammermeier J., Powrie F.,
RA Shah N., Walz C., Nathrath M., Kotlarz D., Puchaka J., Krieger J.R.,
RA Racek T., Kirchner T., Walters T.D., Brumell J.H., Griffiths A.M.,
RA Rezaei N., Rashtian P., Najafi M., Monajemzadeh M., Pelsue S.,
RA McGovern D.P., Uhlig H.H., Schadt E., Klein C., Snapper S.B., Muise A.M.;
RT "Mutations in tetratricopeptide repeat domain 7A result in a severe form of
RT very early onset inflammatory bowel disease.";
RL Gastroenterology 146:1028-1039(2014).
RN [19]
RP VARIANTS GIDID1 ASP-551 AND GLN-828 DEL.
RX PubMed=24931897; DOI=10.1007/s10875-014-0067-7;
RA Agarwal N.S., Northrop L., Anyane-Yeboa K., Aggarwal V.S., Nagy P.L.,
RA Demirdag Y.Y.;
RT "Tetratricopeptide repeat domain 7A (TTC7A) mutation in a newborn with
RT multiple intestinal atresia and combined immunodeficiency.";
RL J. Clin. Immunol. 34:607-610(2014).
RN [20]
RP VARIANTS GIDID1 GLN-277 DEL; TYR-336 DEL; LEU-539 AND ALA-832 DEL.
RX PubMed=24292712; DOI=10.1172/jci71471;
RA Bigorgne A.E., Farin H.F., Lemoine R., Mahlaoui N., Lambert N., Gil M.,
RA Schulz A., Philippet P., Schlesser P., Abrahamsen T.G., Oymar K.,
RA Davies E.G., Ellingsen C.L., Leteurtre E., Moreau-Massart B., Berrebi D.,
RA Bole-Feysot C., Nischke P., Brousse N., Fischer A., Clevers H.,
RA de Saint Basile G.;
RT "TTC7A mutations disrupt intestinal epithelial apicobasal polarity.";
RL J. Clin. Invest. 124:328-337(2014).
RN [21]
RP VARIANT GIDID1 PRO-346.
RX PubMed=25745186; DOI=10.1182/blood-2014-08-595397;
RA Woutsas S., Aytekin C., Salzer E., Conde C.D., Apaydin S., Pichler H.,
RA Memaran-Dadgar N., Hosnut F.O., Foerster-Waldl E., Matthes S., Huber W.D.,
RA Lion T., Holter W., Bilic I., Boztug K.;
RT "Hypomorphic mutation in TTC7A causes combined immunodeficiency with mild
RT structural intestinal defects.";
RL Blood 125:1674-1676(2015).
RN [22]
RP VARIANT GIDID1 GLU-857 DEL.
RX PubMed=25534311; DOI=10.1111/cge.12553;
RA Yang W., Lee P.P., Thong M.K., Ramanujam T.M., Shanmugam A., Koh M.T.,
RA Chan K.W., Ying D., Wang Y., Shen J.J., Yang J., Lau Y.L.;
RT "Compound heterozygous mutations in TTC7A cause familial multiple
RT intestinal atresias and severe combined immunodeficiency.";
RL Clin. Genet. 88:542-549(2015).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane
CC (PubMed:23229899, PubMed:24417819). The complex acts as a regulator of
CC phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In
CC the complex, plays a central role in bridging PI4KA to EFR3B and
CC FAM126A, via direct interactions (By similarity).
CC {ECO:0000250|UniProtKB:Q86TV6, ECO:0000269|PubMed:23229899,
CC ECO:0000269|PubMed:24417819}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC FAM126 (FAM126A or FAM126B) (PubMed:24417819). Interacts with PI4KA
CC (PubMed:34415310). Interaction with PI4KA is direct (By similarity).
CC Interacts with EFR3 (EFR3A or EFR3B), interaction is direct (By
CC similarity). Interacts with FAM126 (FAM126A or FAM126B), interaction is
CC direct (By similarity). Association with the PI4K complex is strongly
CC reduced by TMEM150A (By similarity). {ECO:0000250|UniProtKB:Q86TV6,
CC ECO:0000269|PubMed:24417819, ECO:0000269|PubMed:34415310}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25546680}. Cell
CC membrane {ECO:0000250|UniProtKB:Q86TV6}. Note=Localizes to the cytosol
CC and is recruited to the plasma membrane following interaction with EFR3
CC (EFR3A or EFR3B). {ECO:0000250|UniProtKB:Q86TV6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ULT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULT0-3; Sequence=VSP_039347, VSP_039348;
CC Name=3;
CC IsoId=Q9ULT0-4; Sequence=VSP_057271;
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the intestine,
CC thymus, and pancreas (at protein level). {ECO:0000269|PubMed:25546680}.
CC -!- DISEASE: Gastrointestinal defects and immunodeficiency syndrome 1
CC (GIDID1) [MIM:243150]: An autosomal recessive congenital disorder in
CC which obstructions occur at various levels throughout the small and
CC large intestines, ultimately leading to organ failure. Surgical
CC interventions are palliative but do not provide long-term survival.
CC Some patients exhibit inflammatory bowel disease (IBD), with or without
CC intestinal atresia, and in some cases, the intestinal features are
CC associated with either mild or severe combined immunodeficiency.
CC {ECO:0000269|PubMed:23423984, ECO:0000269|PubMed:23830146,
CC ECO:0000269|PubMed:24292712, ECO:0000269|PubMed:24417819,
CC ECO:0000269|PubMed:24931897, ECO:0000269|PubMed:25534311,
CC ECO:0000269|PubMed:25546680, ECO:0000269|PubMed:25745186}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Phenotypic variations have been observed: the mildest case show
CC intestinal aberrations consisting of bloody diarrhea, apoptotic
CC enterocolitis, and acute graft-versus-host disease- (GVHD)-like
CC symptoms, but no atresias (PubMed:25546680). Other patients show
CC multiple intestinal atresias, some being associated with
CC immunodeficiency syndrome, while other do not show immunodeficiency
CC defects (PubMed:23423984). {ECO:0000269|PubMed:23423984,
CC ECO:0000269|PubMed:25546680}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86454.2; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AL834383; CAD39046.2; -; mRNA.
DR EMBL; AB032966; BAA86454.2; ALT_SEQ; mRNA.
DR EMBL; AC016722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001978; AAH01978.1; -; mRNA.
DR EMBL; BC027457; AAH27457.1; -; mRNA.
DR EMBL; BC111487; AAI11488.1; -; mRNA.
DR CCDS; CCDS33193.1; -. [Q9ULT0-1]
DR CCDS; CCDS74511.1; -. [Q9ULT0-4]
DR RefSeq; NP_001275880.1; NM_001288951.1. [Q9ULT0-4]
DR RefSeq; NP_001275882.1; NM_001288953.1.
DR RefSeq; NP_001275884.1; NM_001288955.1.
DR RefSeq; NP_065191.2; NM_020458.3. [Q9ULT0-1]
DR AlphaFoldDB; Q9ULT0; -.
DR SMR; Q9ULT0; -.
DR BioGRID; 121455; 19.
DR IntAct; Q9ULT0; 8.
DR MINT; Q9ULT0; -.
DR STRING; 9606.ENSP00000378320; -.
DR GlyGen; Q9ULT0; 1 site.
DR iPTMnet; Q9ULT0; -.
DR PhosphoSitePlus; Q9ULT0; -.
DR BioMuta; TTC7A; -.
DR DMDM; 34223742; -.
DR EPD; Q9ULT0; -.
DR jPOST; Q9ULT0; -.
DR MassIVE; Q9ULT0; -.
DR MaxQB; Q9ULT0; -.
DR PaxDb; Q9ULT0; -.
DR PeptideAtlas; Q9ULT0; -.
DR PRIDE; Q9ULT0; -.
DR ProteomicsDB; 61446; -.
DR ProteomicsDB; 85104; -. [Q9ULT0-1]
DR ProteomicsDB; 85105; -. [Q9ULT0-3]
DR Antibodypedia; 47406; 105 antibodies from 19 providers.
DR DNASU; 57217; -.
DR Ensembl; ENST00000319190.11; ENSP00000316699.5; ENSG00000068724.17. [Q9ULT0-1]
DR Ensembl; ENST00000394850.6; ENSP00000378320.2; ENSG00000068724.17. [Q9ULT0-4]
DR GeneID; 57217; -.
DR KEGG; hsa:57217; -.
DR MANE-Select; ENST00000319190.11; ENSP00000316699.5; NM_020458.4; NP_065191.2.
DR UCSC; uc002rvo.4; human. [Q9ULT0-1]
DR CTD; 57217; -.
DR DisGeNET; 57217; -.
DR GeneCards; TTC7A; -.
DR HGNC; HGNC:19750; TTC7A.
DR HPA; ENSG00000068724; Tissue enhanced (testis).
DR MalaCards; TTC7A; -.
DR MIM; 243150; phenotype.
DR MIM; 609332; gene.
DR neXtProt; NX_Q9ULT0; -.
DR OpenTargets; ENSG00000068724; -.
DR Orphanet; 436252; Combined immunodeficiency-enteropathy spectrum.
DR Orphanet; 2300; Multiple intestinal atresia.
DR PharmGKB; PA134993362; -.
DR VEuPathDB; HostDB:ENSG00000068724; -.
DR eggNOG; KOG4162; Eukaryota.
DR GeneTree; ENSGT00940000158638; -.
DR HOGENOM; CLU_010512_1_0_1; -.
DR InParanoid; Q9ULT0; -.
DR OMA; WYRRIMT; -.
DR OrthoDB; 167932at2759; -.
DR PhylomeDB; Q9ULT0; -.
DR TreeFam; TF313783; -.
DR PathwayCommons; Q9ULT0; -.
DR SignaLink; Q9ULT0; -.
DR BioGRID-ORCS; 57217; 76 hits in 1080 CRISPR screens.
DR ChiTaRS; TTC7A; human.
DR GenomeRNAi; 57217; -.
DR Pharos; Q9ULT0; Tbio.
DR PRO; PR:Q9ULT0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULT0; protein.
DR Bgee; ENSG00000068724; Expressed in sperm and 165 other tissues.
DR ExpressionAtlas; Q9ULT0; baseline and differential.
DR Genevisible; Q9ULT0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR045819; TTC7_N.
DR InterPro; IPR026900; Ttc7A.
DR PANTHER; PTHR23083:SF475; PTHR23083:SF475; 1.
DR Pfam; PF13181; TPR_8; 2.
DR Pfam; PF19440; TTC7_N; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disease variant; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..858
FT /note="Tetratricopeptide repeat protein 7A"
FT /id="PRO_0000106385"
FT REPEAT 121..157
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 177..210
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 414..447
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 497..531
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 533..565
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 566..599
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 745..778
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 780..812
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REPEAT 813..846
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGB2"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGB2"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 117..146
FT /note="PQYMCEAMLILGKLHYVEGSYRDAISMYAR -> GLAVLLRLVSNSWAQAIL
FT LLQPPEALGLQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_039347"
FT VAR_SEQ 147..858
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_039348"
FT VAR_SEQ 639
FT /note="L -> LGDFRSPEGFQTPQRNICNSEIYRG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057271"
FT VARIANT 71
FT /note="E -> K (in GIDID1; reduced interaction with PI4KA;
FT dbSNP:rs147914967)"
FT /evidence="ECO:0000269|PubMed:24417819"
FT /id="VAR_075126"
FT VARIANT 277
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24292712"
FT /id="VAR_075127"
FT VARIANT 336
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24292712"
FT /id="VAR_075128"
FT VARIANT 346
FT /note="L -> P (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:25745186"
FT /id="VAR_075129"
FT VARIANT 399
FT /note="L -> P (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:23830146"
FT /id="VAR_075130"
FT VARIANT 526
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24417819"
FT /id="VAR_075131"
FT VARIANT 538
FT /note="V -> L (in dbSNP:rs2304290)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_016602"
FT VARIANT 539
FT /note="S -> L (in GIDID1; dbSNP:rs776906926)"
FT /evidence="ECO:0000269|PubMed:24292712"
FT /id="VAR_075132"
FT VARIANT 545
FT /note="V -> I (in dbSNP:rs6755258)"
FT /id="VAR_052624"
FT VARIANT 551
FT /note="A -> D (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24931897"
FT /id="VAR_075133"
FT VARIANT 606
FT /note="K -> R (in GIDID1; dbSNP:rs139010200)"
FT /evidence="ECO:0000269|PubMed:23830146"
FT /id="VAR_075134"
FT VARIANT 672
FT /note="S -> P (in GIDID1; dbSNP:rs149602485)"
FT /evidence="ECO:0000269|PubMed:23830146"
FT /id="VAR_075135"
FT VARIANT 678
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:23830146"
FT /id="VAR_075136"
FT VARIANT 712
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:23830146"
FT /id="VAR_075137"
FT VARIANT 823
FT /note="L -> P (in GIDID1; dbSNP:rs587776972)"
FT /evidence="ECO:0000269|PubMed:23423984,
FT ECO:0000269|PubMed:23830146"
FT /id="VAR_069636"
FT VARIANT 828
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24931897"
FT /id="VAR_075138"
FT VARIANT 832
FT /note="A -> T (in GIDID1; reduced interaction with PI4KA;
FT dbSNP:rs876657393)"
FT /evidence="ECO:0000269|PubMed:24417819"
FT /id="VAR_075139"
FT VARIANT 832
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:24292712"
FT /id="VAR_075140"
FT VARIANT 857
FT /note="Missing (in GIDID1)"
FT /evidence="ECO:0000269|PubMed:25534311"
FT /id="VAR_075141"
FT CONFLICT 603
FT /note="M -> I (in Ref. 2; BAA86454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 96185 MW; 9D10411B48478171 CRC64;
MAAKGAHGSY LKVESELERC RAEGHWDRMP ELVRQLQTLS MPGGGGNRRG SPSAAFTFPD
TDDFGKLLLA EALLEQCLKE NHAKIKDSMP LLEKNEPKMS EAKNYLSSIL NHGRLSPQYM
CEAMLILGKL HYVEGSYRDA ISMYARAGID DMSMENKPLY QMRLLSEAFV IKGLSLERLP
NSIASRFRLT EREEEVITCF ERASWIAQVF LQELEKTTNN STSRHLKGCH PLDYELTYFL
EAALQSAYVK NLKKGNIVKG MRELREVLRT VETKATQNFK VMAAKHLAGV LLHSLSEECY
WSPLSHPLPE FMGKEESSFA TQALRKPHLY EGDNLYCPKD NIEEALLLLL ISESMATRDV
VLSRVPEQEE DRTVSLQNAA AIYDLLSITL GRRGQYVMLS ECLERAMKFA FGEFHLWYQV
ALSMVACGKS AYAVSLLREC VKLRPSDPTV PLMAAKVCIG SLRWLEEAEH FAMMVISLGE
EAGEFLPKGY LALGLTYSLQ ATDATLKSKQ DELHRKALQT LERAQQLAPS DPQVILYVSL
QLALVRQISS AMEQLQEALK VRKDDAHALH LLALLFSAQK HHQHALDVVN MAITEHPENF
NLMFTKVKLE QVLKGPEEAL VTCRQVLRLW QTLYSFSQLG GLEKDGSFGE GLTMKKQSGM
HLTLPDAHDA DSGSRRASSI AASRLEEAMS ELTMPSSVLK QGPMQLWTTL EQIWLQAAEL
FMEQQHLKEA GFCIQEAAGL FPTSHSVLYM RGRLAEVKGN LEEAKQLYKE ALTVNPDGVR
IMHSLGLMLS RLGHKSLAQK VLRDAVERQS TCHEAWQGLG EVLQAQGQNE AAVDCFLTAL
ELEASSPVLP FSIIPREL
