TTC7A_MOUSE
ID TTC7A_MOUSE Reviewed; 858 AA.
AC Q8BGB2; Q80XT5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tetratricopeptide repeat protein 7A;
DE Short=TPR repeat protein 7A;
GN Name=Ttc7a; Synonyms=Ttc7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-678; SER-679;
RP SER-690 AND THR-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The
CC complex acts as a regulator of phosphatidylinositol 4-phosphate
CC (PtdIns(4)P) synthesis (By similarity). In the complex, plays a central
CC role in bridging PI4KA to EFR3B and FAM126A, via direct interactions
CC (By similarity). {ECO:0000250|UniProtKB:Q86TV6,
CC ECO:0000250|UniProtKB:Q9ULT0}.
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) (By similarity). Interacts with PI4KA,
CC interaction is direct (By similarity). Interacts with EFR3 (EFR3A or
CC EFR3B), interaction is direct (By similarity). Interacts with FAM126
CC (FAM126A or FAM126B), interaction is direct (By similarity).
CC Association with the PI4K complex is strongly reduced by TMEM150A (By
CC similarity). {ECO:0000250|UniProtKB:Q86TV6,
CC ECO:0000250|UniProtKB:Q9ULT0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULT0}. 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}.
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DR EMBL; AK040578; BAC30634.1; -; mRNA.
DR EMBL; AK050263; BAC34153.1; -; mRNA.
DR EMBL; AK080284; BAC37865.1; -; mRNA.
DR EMBL; BC042512; AAH42512.2; -; mRNA.
DR CCDS; CCDS29016.1; -.
DR RefSeq; NP_082915.1; NM_028639.3.
DR AlphaFoldDB; Q8BGB2; -.
DR SMR; Q8BGB2; -.
DR BioGRID; 230355; 5.
DR STRING; 10090.ENSMUSP00000040771; -.
DR iPTMnet; Q8BGB2; -.
DR PhosphoSitePlus; Q8BGB2; -.
DR EPD; Q8BGB2; -.
DR jPOST; Q8BGB2; -.
DR MaxQB; Q8BGB2; -.
DR PaxDb; Q8BGB2; -.
DR PeptideAtlas; Q8BGB2; -.
DR PRIDE; Q8BGB2; -.
DR ProteomicsDB; 300156; -.
DR Antibodypedia; 47406; 105 antibodies from 19 providers.
DR Ensembl; ENSMUST00000041110; ENSMUSP00000040771; ENSMUSG00000036918.
DR GeneID; 225049; -.
DR KEGG; mmu:225049; -.
DR UCSC; uc008duv.2; mouse.
DR CTD; 225049; -.
DR MGI; MGI:1920999; Ttc7.
DR VEuPathDB; HostDB:ENSMUSG00000036918; -.
DR eggNOG; KOG4162; Eukaryota.
DR GeneTree; ENSGT00940000158638; -.
DR HOGENOM; CLU_010512_1_0_1; -.
DR InParanoid; Q8BGB2; -.
DR OMA; WYRRIMT; -.
DR OrthoDB; 167932at2759; -.
DR PhylomeDB; Q8BGB2; -.
DR TreeFam; TF313783; -.
DR BioGRID-ORCS; 225049; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ttc7; mouse.
DR PRO; PR:Q8BGB2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BGB2; protein.
DR Bgee; ENSMUSG00000036918; Expressed in granulocyte and 131 other tissues.
DR ExpressionAtlas; Q8BGB2; baseline and differential.
DR Genevisible; Q8BGB2; MM.
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; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS: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; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..858
FT /note="Tetratricopeptide repeat protein 7A"
FT /id="PRO_0000106386"
FT REPEAT 122..158
FT /note="TPR 1"
FT REPEAT 415..448
FT /note="TPR 2"
FT REPEAT 498..532
FT /note="TPR 3"
FT REPEAT 533..566
FT /note="TPR 4"
FT REPEAT 567..600
FT /note="TPR 5"
FT REPEAT 745..778
FT /note="TPR 6"
FT REPEAT 779..812
FT /note="TPR 7"
FT REPEAT 813..846
FT /note="TPR 8"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT0"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULT0"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 858 AA; 96156 MW; AEE2C01FA7CA3589 CRC64;
MAAKGAHGTH LKVESEVERC RAEGQWDRMF ELARHLQMLG ISGGGSSNRR NSPSGRFTTL
DTDDFVKLLL AEALLEQCLK DNHDKIKNSI PLLEKTDHRL NEAKDHLSSL LNNGKLPPQY
MCEAMLILGK LHYVEGSYRD AVSMYARAGI DDISVENKPL YQMRLLSEAF VIKGLSLERL
PNSVASHIRL TEREEEVVAC FERASWVAQV FLQELEKTSN NSTSRHLKGS LSPDYELSYF
LEAALQSAYV KNLKKGNIVK GMRELREILR TVETKATQNF KVVAAKHLAG VLLHSLSEDC
YWSPLSHPLP EFMNKEENSF VTQTLRKPHL YEGDNLYCPK DNIEEALLLL LISESMATRD
VVLSRAPEQA EDRKVSLQNA SAIYDLLSIT LGRRGQYVML SECLERAMKC AFGEFHLWYQ
VALSMVACGK SAYAVSLLRE CMKLQPSDPT VPLMAAKVCI GSLHWLEEAE HFATVVIGLG
EEAGESLPKG YLALGLTYSL QATDATLKSK QDELHRKALQ TLERARELAP DDPQIIFYVA
LQLALVRQIS SAMERLQEAL TMCRDDANAL HLLALLFSAQ KYYQHALDVI NMAITEHPEN
FNLMFTKVKL EQVLKGPEEA LVTCRQMLRL WQTLYNFSQL GGLEKDGSFE GLTVKKQNGI
HLTLPDAHDA DSGSRRASSI AASRLEEAMS ELTLTTSVLK QGPMQLWTTL EQIWLQAAEL
FMEQRQLKEA GFCIQEAAGL FPTSHSVLYM RGRLAEVKGS FEEAKQLYKE ALTVNPDGVR
IMHSLGLMLS QLGHKSLAQK VLRDAVERQS TFHEAWQGLG EVLQDQGQNE AAVDCFLTAL
ELEASSPVLP FSIIAREL
