MON1A_HUMAN
ID MON1A_HUMAN Reviewed; 652 AA.
AC Q86VX9; B2RDQ1; G5E9N1; Q8NAV7; Q9BRF3; X6R3V9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Vacuolar fusion protein MON1 homolog A;
GN Name=MON1A; Synonyms=SAND1;
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] (ISOFORMS 3 AND 5).
RC TISSUE=Synovial cell;
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 GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Brain, Lung, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP 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 [6]
RP IDENTIFICATION BY 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 [7]
RP FUNCTION, AND INTERACTION WITH CCZ1.
RX PubMed=23084991; DOI=10.1016/j.cub.2012.09.020;
RA Gerondopoulos A., Langemeyer L., Liang J.R., Linford A., Barr F.A.;
RT "BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine
RT nucleotide exchange factor.";
RL Curr. Biol. 22:2135-2139(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; THR-158 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
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 [10]
RP IDENTIFICATION IN A COMPLEX WITH RMC1; CCZ1; MON1A AND MON1B.
RX PubMed=29038162; DOI=10.1128/mcb.00392-17;
RA Pontano Vaites L., Paulo J.A., Huttlin E.L., Harper J.W.;
RT "Systematic analysis of human cells lacking ATG8 proteins uncovers roles
RT for GABARAPs and the CCZ1/MON1 regulator C18orf8/RMC1 in macro and
RT selective autophagic flux.";
RL Mol. Cell. Biol. 0:0-0(2017).
RN [11]
RP INTERACTION OF MON1A/CCZ1B COMPLEX WITH RIMOC1 AND RAB7A.
RX PubMed=34432599; DOI=10.1080/15548627.2021.1960116;
RA Yan B.R., Li T., Coyaud E., Laurent E.M.N., St-Germain J., Zhou Y.,
RA Kim P.K., Raught B., Brumell J.H.;
RT "C5orf51 is a component of the MON1-CCZ1 complex and controls RAB7A
RT localization and stability during mitophagy.";
RL Autophagy 18:829-840(2022).
CC -!- FUNCTION: Plays an important role in membrane trafficking through the
CC secretory apparatus. Not involved in endocytic trafficking to lysosomes
CC (By similarity). Acts in concert with CCZ1, as a guanine exchange
CC factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting
CC it from an inactive GDP-bound form into an active GTP-bound form
CC (PubMed:23084991). {ECO:0000250|UniProtKB:Q6PDG8,
CC ECO:0000269|PubMed:23084991}.
CC -!- SUBUNIT: Interacts with CCZ1 (PubMed:23084991). Found in a complex with
CC RMC1, CCZ1, MON1A and MON1B (PubMed:29038162). The MON1A-CCZ1B complex
CC interacts with RIMOC1 (PubMed:34432599). The MON1A-CCZ1B complex
CC interacts with RAB7A and this interaction is enhanced in the presence
CC of RIMOC1 (PubMed:34432599). {ECO:0000269|PubMed:23084991,
CC ECO:0000269|PubMed:29038162, ECO:0000269|PubMed:34432599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86VX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VX9-2; Sequence=VSP_059430, VSP_059431;
CC Name=3;
CC IsoId=Q86VX9-3; Sequence=VSP_059430, VSP_059431, VSP_059432,
CC VSP_059433;
CC Name=4;
CC IsoId=Q86VX9-4; Sequence=VSP_059431;
CC Name=5;
CC IsoId=Q86VX9-5; Sequence=VSP_059430;
CC -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47022.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK092018; BAC03790.1; -; mRNA.
DR EMBL; AK315630; BAG37998.1; -; mRNA.
DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65037.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65038.1; -; Genomic_DNA.
DR EMBL; BC006299; AAH06299.1; -; mRNA.
DR EMBL; BC009459; AAH09459.1; -; mRNA.
DR EMBL; BC047022; AAH47022.1; ALT_INIT; mRNA.
DR CCDS; CCDS2808.2; -. [Q86VX9-5]
DR CCDS; CCDS46830.1; -. [Q86VX9-2]
DR RefSeq; NP_001135973.1; NM_001142501.1. [Q86VX9-2]
DR RefSeq; NP_115731.2; NM_032355.3. [Q86VX9-1]
DR RefSeq; XP_006713408.1; XM_006713345.3. [Q86VX9-5]
DR RefSeq; XP_011532462.1; XM_011534160.1. [Q86VX9-5]
DR AlphaFoldDB; Q86VX9; -.
DR SMR; Q86VX9; -.
DR BioGRID; 124041; 13.
DR IntAct; Q86VX9; 9.
DR MINT; Q86VX9; -.
DR STRING; 9606.ENSP00000296473; -.
DR iPTMnet; Q86VX9; -.
DR PhosphoSitePlus; Q86VX9; -.
DR BioMuta; MON1A; -.
DR DMDM; 146324996; -.
DR EPD; Q86VX9; -.
DR jPOST; Q86VX9; -.
DR MassIVE; Q86VX9; -.
DR MaxQB; Q86VX9; -.
DR PaxDb; Q86VX9; -.
DR PeptideAtlas; Q86VX9; -.
DR PRIDE; Q86VX9; -.
DR ProteomicsDB; 33990; -.
DR ProteomicsDB; 70086; -. [Q86VX9-1]
DR ProteomicsDB; 70087; -. [Q86VX9-2]
DR ProteomicsDB; 70088; -. [Q86VX9-3]
DR Antibodypedia; 46026; 169 antibodies from 27 providers.
DR DNASU; 84315; -.
DR Ensembl; ENST00000296473.8; ENSP00000296473.4; ENSG00000164077.15. [Q86VX9-5]
DR Ensembl; ENST00000417270.2; ENSP00000399613.2; ENSG00000164077.15. [Q86VX9-5]
DR Ensembl; ENST00000455683.7; ENSP00000404793.3; ENSG00000164077.15. [Q86VX9-2]
DR Ensembl; ENST00000642691.1; ENSP00000494294.1; ENSG00000164077.15. [Q86VX9-5]
DR Ensembl; ENST00000645862.1; ENSP00000494452.1; ENSG00000164077.15. [Q86VX9-5]
DR GeneID; 84315; -.
DR KEGG; hsa:84315; -.
DR MANE-Select; ENST00000296473.8; ENSP00000296473.4; NM_032355.4; NP_115731.3. [Q86VX9-5]
DR UCSC; uc003cxz.4; human.
DR UCSC; uc003cya.4; human. [Q86VX9-1]
DR CTD; 84315; -.
DR DisGeNET; 84315; -.
DR GeneCards; MON1A; -.
DR HGNC; HGNC:28207; MON1A.
DR HPA; ENSG00000164077; Low tissue specificity.
DR MIM; 611464; gene.
DR neXtProt; NX_Q86VX9; -.
DR OpenTargets; ENSG00000164077; -.
DR PharmGKB; PA142671340; -.
DR VEuPathDB; HostDB:ENSG00000164077; -.
DR eggNOG; KOG0997; Eukaryota.
DR GeneTree; ENSGT00390000006665; -.
DR HOGENOM; CLU_014574_1_1_1; -.
DR InParanoid; Q86VX9; -.
DR OMA; TNSTCEY; -.
DR OrthoDB; 829786at2759; -.
DR PhylomeDB; Q86VX9; -.
DR TreeFam; TF314665; -.
DR PathwayCommons; Q86VX9; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q86VX9; -.
DR BioGRID-ORCS; 84315; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; MON1A; human.
DR GenomeRNAi; 84315; -.
DR Pharos; Q86VX9; Tbio.
DR PRO; PR:Q86VX9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q86VX9; protein.
DR Bgee; ENSG00000164077; Expressed in prefrontal cortex and 164 other tissues.
DR ExpressionAtlas; Q86VX9; baseline and differential.
DR Genevisible; Q86VX9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR InterPro; IPR004353; Mon1.
DR PANTHER; PTHR13027; PTHR13027; 1.
DR Pfam; PF19036; Fuz_longin_1; 1.
DR Pfam; PF19037; Fuz_longin_2; 1.
DR Pfam; PF19038; Fuz_longin_3; 1.
DR PRINTS; PR01546; YEAST73DUF.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..652
FT /note="Vacuolar fusion protein MON1 homolog A"
FT /id="PRO_0000285761"
FT REGION 102..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDG8"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 5, isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_059430"
FT VAR_SEQ 140..301
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_059431"
FT VAR_SEQ 557
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059432"
FT VAR_SEQ 558..652
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059433"
SQ SEQUENCE 652 AA; 72895 MW; 344D326577E66FE2 CRC64;
MHPGGGPSRA ERLELGLGRE RPAKAIFLHR RPGEGGGRER CLRCGHVCVR RGPGPREAVP
SGRPRPDTLT PPWVRQRAVT GTFCASWTPL RNRRAQRMAT DMQRKRSSEC LDGTLTPSDG
QSMERAESPT PGMAQGMEPG AGQEGAMFVH ARSYEDLTES EDGAASGDSH KEGTRGPPPL
PTDMRQISQD FSELSTQLTG VARDLQEEML PGSSEDWLEP PGAVGRPATE PPREGTTEGD
EEDATEAWRL HQKHVFVLSE AGKPVYSRYG SEEALSSTMG VMVALVSFLE ADKNAIRSIH
ADGYKVVFVR RSPLVLVAVA RTRQSAQELA QELLYIYYQI LSLLTGAQLS HIFQQKQNYD
LRRLLSGSER ITDNLLQLMA RDPSFLMGAA RCLPLAAAVR DTVSASLQQA RARSLVFSIL
LARNQLVALV RRKDQFLHPI DLHLLFNLIS SSSSFREGEA WTPVCLPKFN AAGFFHAHIS
YLEPDTDLCL LLVSTDREDF FAVSDCRRRF QERLRKRGAH LALREALRTP YYSVAQVGIP
DLRHFLYKSK SSGLFTSPEI EAPYTSEEEQ ERLLGLYQYL HSRAHNASRP LKTIYYTGPN
ENLLAWVTGA FELYMCYSPL GTKASAVSAI HKLMRWIRKE EDRLFILTPL TY
