ID F6Y2X3_HUMAN Unreviewed; 262 AA.
AC F6Y2X3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN Name=TAFAZZIN {ECO:0000313|Ensembl:ENSP00000358791.4};
GN Synonyms=TAZ {ECO:0000256|RuleBase:RU365062,
GN ECO:0000313|EMBL:ALQ33806.1};
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 {ECO:0000313|Ensembl:ENSP00000358791.4, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000358791.4, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2] {ECO:0000313|EMBL:ALQ33806.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26871637; DOI=10.1016/j.cell.2016.01.029;
RA Yang X., Coulombe-Huntington J., Kang S., Sheynkman G.M., Hao T.,
RA Richardson A., Sun S., Yang F., Shen Y.A., Murray R., Spirohn K.,
RA Begg B.E., Duran-Frigola M., MacWilliams A., Pevzner S.J., Zhong Q.,
RA Trigg S.A., Tam S., Ghamsari L., Sahni N., Yi S., Rodriguez M.D.,
RA Balcha D., Tan G., Costanzo M., Andrews B., Boone C., Zhou X.J.,
RA Salehi-Ashtiani K., Charloteaux B., Chen A., Calderwood M.A., Aloy P.,
RA Roth F.P., Hill D.E., Iakoucheva L.M., Xia Y., Vidal M.;
RT "Widespread Expansion of Protein Interaction Capabilities by Alternative
RT Splicing.";
RL Cell 164:805-817(2016).
RN [3] {ECO:0000313|Ensembl:ENSP00000358791.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Acyltransferase which is required to remodel newly
CC synthesized phospholipid cardiolipin, a key component of the
CC mitochondrial inner membrane. Required for the initiation of mitophagy.
CC Required to ensure progression of spermatocytes through meiosis.
CC {ECO:0000256|RuleBase:RU365062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:43816, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000256|ARBA:ARBA00024577};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000256|ARBA:ARBA00024577};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000256|ARBA:ARBA00024577};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1-acyl-
CC sn-glycero-3-phosphate = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)
CC + a 1,2-diacyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:67748,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58608, ChEBI:CHEBI:64716,
CC ChEBI:CHEBI:64840; Evidence={ECO:0000256|ARBA:ARBA00024592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000256|ARBA:ARBA00024592};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000256|ARBA:ARBA00024592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + 1-hexadecanoyl-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-
CC (9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate +
CC 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol);
CC Xref=Rhea:RHEA:67752, ChEBI:CHEBI:72840, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74563, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000256|ARBA:ARBA00024553};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000256|ARBA:ARBA00024553};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000256|ARBA:ARBA00024553};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + 2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:68988,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:76084; Evidence={ECO:0000256|ARBA:ARBA00029361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989;
CC Evidence={ECO:0000256|ARBA:ARBA00029361};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990;
CC Evidence={ECO:0000256|ARBA:ARBA00029361};
CC -!- SUBUNIT: Associates with multiple protein complexes.
CC {ECO:0000256|ARBA:ARBA00024371}.
CC -!- INTERACTION:
CC F6Y2X3; P27797: CALR; NbExp=3; IntAct=EBI-25833693, EBI-1049597;
CC F6Y2X3; P36957: DLST; NbExp=3; IntAct=EBI-25833693, EBI-351007;
CC F6Y2X3; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-25833693, EBI-1055945;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00024323}.
CC -!- SIMILARITY: Belongs to the taffazin family.
CC {ECO:0000256|ARBA:ARBA00010524, ECO:0000256|RuleBase:RU365062}.
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DR EMBL; AC244090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC245140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KU178348; ALQ33806.1; -; mRNA.
DR IntAct; F6Y2X3; 3.
DR Antibodypedia; 31212; 488 antibodies from 37 providers.
DR Ensembl; ENST00000369776.8; ENSP00000358791.4; ENSG00000102125.17.
DR HGNC; HGNC:11577; TAFAZZIN.
DR VEuPathDB; HostDB:ENSG00000102125; -.
DR GeneTree; ENSGT00390000018621; -.
DR ChiTaRS; TAZ; human.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000102125; Expressed in apex of heart and 163 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497:SF0; TAFAZZIN; 1.
DR PANTHER; PTHR12497; TAZ PROTEIN TAFAZZIN; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Proteomics identification {ECO:0007829|EPD:F6Y2X3,
KW ECO:0007829|MaxQB:F6Y2X3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 68..126
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF01553"
SQ SEQUENCE 262 AA; 28966 MW; 80C888D77DFBEE55 CRC64;
MPLHVKWPFP AVPPLTWTLA SSVVMGLVGT YSCFWTSEWA QAEAGPPGYP CPAGGILKLR
HIWNLKLMRW TPAAADICFT KELHSHFFSL GKCVPVCRGD GVYQKGMDFI LEKLNHGDWV
HIFPEGIGRL IAECHLNPII LPLWHVGEPG DGDREMASGV GGLGLPLVPG CPAPPHVWPS
VHCAAGMNDV LPNSPPYFPR FGQKITVLIG KPFSALPVLE RLRAENKSAV EMRKALTDFI
QEEFQHLKTQ AEQLHNHLQP GR
//
