MTX3_HUMAN
ID MTX3_HUMAN Reviewed; 312 AA.
AC Q5HYI7; B4DL65; E9PB57; Q7Z380; Q8NB92;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Metaxin-3;
GN Name=MTX3;
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 3).
RC TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Fetal skin, and Retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-284 AND SER-311, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [8]
RP IDENTIFICATION IN THE MIB COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=26477565; DOI=10.1016/j.bbamcr.2015.10.009;
RA Huynen M.A., Muehlmeister M., Gotthardt K., Guerrero-Castillo S.,
RA Brandt U.;
RT "Evolution and structural organization of the mitochondrial contact site
RT (MICOS) complex and the mitochondrial intermembrane space bridging (MIB)
RT complex.";
RL Biochim. Biophys. Acta 1863:91-101(2016).
CC -!- FUNCTION: Could function in transport of proteins into the
CC mitochondrion. {ECO:0000250}.
CC -!- SUBUNIT: Part of a large protein complex spanning both mitochondrial
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex. {ECO:0000305|PubMed:26477565}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:26477565}.
CC Mitochondrion outer membrane {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5HYI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HYI7-2; Sequence=VSP_033893, VSP_033894;
CC Name=3;
CC IsoId=Q5HYI7-4; Sequence=VSP_036207, VSP_036208;
CC Name=4;
CC IsoId=Q5HYI7-5; Sequence=VSP_046824;
CC -!- SIMILARITY: Belongs to the metaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97995.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK296864; BAG59427.1; -; mRNA.
DR EMBL; BX538064; CAD97995.1; ALT_INIT; mRNA.
DR EMBL; BX647596; CAI46098.1; -; mRNA.
DR EMBL; AC112184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47239.2; -. [Q5HYI7-4]
DR CCDS; CCDS54872.1; -. [Q5HYI7-5]
DR CCDS; CCDS87308.1; -. [Q5HYI7-1]
DR RefSeq; NP_001010891.4; NM_001010891.4. [Q5HYI7-4]
DR RefSeq; NP_001161213.1; NM_001167741.1. [Q5HYI7-5]
DR RefSeq; XP_005248552.1; XM_005248495.3.
DR AlphaFoldDB; Q5HYI7; -.
DR SMR; Q5HYI7; -.
DR BioGRID; 131365; 86.
DR IntAct; Q5HYI7; 29.
DR STRING; 9606.ENSP00000423600; -.
DR iPTMnet; Q5HYI7; -.
DR PhosphoSitePlus; Q5HYI7; -.
DR BioMuta; MTX3; -.
DR DMDM; 189029218; -.
DR EPD; Q5HYI7; -.
DR jPOST; Q5HYI7; -.
DR MassIVE; Q5HYI7; -.
DR MaxQB; Q5HYI7; -.
DR PaxDb; Q5HYI7; -.
DR PeptideAtlas; Q5HYI7; -.
DR PRIDE; Q5HYI7; -.
DR ProteomicsDB; 19149; -.
DR ProteomicsDB; 62935; -. [Q5HYI7-1]
DR ProteomicsDB; 62936; -. [Q5HYI7-2]
DR ProteomicsDB; 62937; -. [Q5HYI7-4]
DR Antibodypedia; 61562; 38 antibodies from 11 providers.
DR DNASU; 345778; -.
DR Ensembl; ENST00000509852.6; ENSP00000423302.1; ENSG00000177034.17. [Q5HYI7-4]
DR Ensembl; ENST00000512528.3; ENSP00000424798.2; ENSG00000177034.17. [Q5HYI7-1]
DR Ensembl; ENST00000512560.5; ENSP00000423600.1; ENSG00000177034.17. [Q5HYI7-5]
DR Ensembl; ENST00000617335.4; ENSP00000484157.1; ENSG00000177034.17. [Q5HYI7-2]
DR GeneID; 345778; -.
DR KEGG; hsa:345778; -.
DR MANE-Select; ENST00000512528.3; ENSP00000424798.2; NM_001363818.2; NP_001350747.1.
DR UCSC; uc003kge.5; human. [Q5HYI7-1]
DR CTD; 345778; -.
DR DisGeNET; 345778; -.
DR GeneCards; MTX3; -.
DR HGNC; HGNC:24812; MTX3.
DR HPA; ENSG00000177034; Low tissue specificity.
DR MIM; 619336; gene.
DR neXtProt; NX_Q5HYI7; -.
DR OpenTargets; ENSG00000177034; -.
DR PharmGKB; PA134924631; -.
DR VEuPathDB; HostDB:ENSG00000177034; -.
DR eggNOG; KOG3028; Eukaryota.
DR GeneTree; ENSGT00950000182919; -.
DR HOGENOM; CLU_044137_5_2_1; -.
DR InParanoid; Q5HYI7; -.
DR OMA; ANYFFGN; -.
DR OrthoDB; 1472286at2759; -.
DR PhylomeDB; Q5HYI7; -.
DR TreeFam; TF313422; -.
DR PathwayCommons; Q5HYI7; -.
DR SignaLink; Q5HYI7; -.
DR BioGRID-ORCS; 345778; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; MTX3; human.
DR GenomeRNAi; 345778; -.
DR Pharos; Q5HYI7; Tdark.
DR PRO; PR:Q5HYI7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q5HYI7; protein.
DR Bgee; ENSG00000177034; Expressed in oviduct epithelium and 186 other tissues.
DR Genevisible; Q5HYI7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR017410; Metaxin1/3.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR019564; Sam37/metaxin_N.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF10568; Tom37; 1.
DR PIRSF; PIRSF038150; Metaxin; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..312
FT /note="Metaxin-3"
FT /id="PRO_0000337100"
FT REGION 278..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_046824"
FT VAR_SEQ 144..158
FT /note="KGALNRILLTRGQPP -> QQILSSRAGTHMLRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033893"
FT VAR_SEQ 159..312
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033894"
FT VAR_SEQ 247..248
FT /note="GI -> DG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036207"
FT VAR_SEQ 249..312
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036208"
FT VARIANT 238
FT /note="S -> R (in dbSNP:rs9293796)"
FT /id="VAR_043600"
FT CONFLICT 50
FT /note="R -> K (in Ref. 2; CAI46098)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35093 MW; 3B9BAB7CF64FF8EF CRC64;
MAAPLELSCW GGGWGLPSVH SESLVVMAYA KFSGAPLKVN VIDNTWRGSR GDVPILTTED
DMVSQPAKIL NFLRKQKYNA DYELSAKQGA DTLAYIALLE EKLLPAVLHT FWVESDNYFT
VTKPWFASQI PFPLSLILPG RMSKGALNRI LLTRGQPPLY HLREVEAQIY RDAKECLNLL
SNRLGTSQFF FGDTPSTLDA YVFGFLAPLY KVRFPKVQLQ EHLKQLSNLC RFCDDILSSY
FRLSLGGISP AGQETVDANL QKLTQLVNKE SNLIEKMDDN LRQSPQLPPR KLPTLKLTPA
EEENNSFQRL SP
