ID   MON1A_MOUSE             Reviewed;         556 AA.
AC   Q6PDG8; Q80UP6; Q9CYS2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   08-NOV-2023, entry version 112.
DE   RecName: Full=Vacuolar fusion protein MON1 homolog A;
GN   Name=Mon1a;
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and Mammary tumor;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   FUNCTION, VARIANT SER-374, AND TISSUE SPECIFICITY.
RX   PubMed=17632513; DOI=10.1038/ng2059;
RA   Wang F., Paradkar P.N., Custodio A.O., McVey Ward D., Fleming M.D.,
RA   Campagna D., Roberts K.A., Boyartchuk V., Dietrich W.F., Kaplan J.,
RA   Andrews N.C.;
RT   "Genetic variation in Mon1a affects protein trafficking and modifies
RT   macrophage iron loading in mice.";
RL   Nat. Genet. 39:1025-1032(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-56; SER-79 AND
RP   SER-91, AND IDENTIFICATION BY 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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: Plays an important role in membrane trafficking through the
CC       secretory apparatus. Not involved in endocytic trafficking to lysosomes
CC       (PubMed:17632513). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q86VX9,
CC       ECO:0000269|PubMed:17632513}.
CC   -!- SUBUNIT: Interacts with CCZ1 (By similarity). Found in a complex with
CC       RMC1, CCZ1, MON1A and MON1B (By similarity). The MON1A-CCZ1B complex
CC       interacts with RIMOC1 (By similarity). The MON1A-CCZ1B complex
CC       interacts with RAB7A and this interaction is enhanced in the presence
CC       of RIMOC1 (By similarity). {ECO:0000250|UniProtKB:Q86VX9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PDG8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDG8-2; Sequence=VSP_024913, VSP_024914;
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       {ECO:0000269|PubMed:17632513}.
CC   -!- POLYMORPHISM: The variant Ser-374 is unique to C57BL strains. It may
CC       confer the low iron phenotype observed in these strains.
CC       {ECO:0000269|PubMed:17632513}.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family. {ECO:0000305}.
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DR   EMBL; AK013387; BAB28823.1; -; mRNA.
DR   EMBL; AK172624; BAE43102.1; -; mRNA.
DR   EMBL; BC048852; AAH48852.1; -; mRNA.
DR   EMBL; BC058717; AAH58717.1; -; mRNA.
DR   CCDS; CCDS23508.1; -. [Q6PDG8-1]
DR   RefSeq; NP_082645.1; NM_028369.3.
DR   RefSeq; XP_017169099.1; XM_017313610.1.
DR   AlphaFoldDB; Q6PDG8; -.
DR   SMR; Q6PDG8; -.
DR   BioGRID; 215589; 3.
DR   STRING; 10090.ENSMUSP00000035202; -.
DR   GlyGen; Q6PDG8; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q6PDG8; -.
DR   PhosphoSitePlus; Q6PDG8; -.
DR   EPD; Q6PDG8; -.
DR   jPOST; Q6PDG8; -.
DR   MaxQB; Q6PDG8; -.
DR   PaxDb; 10090-ENSMUSP00000035202; -.
DR   PeptideAtlas; Q6PDG8; -.
DR   ProteomicsDB; 290096; -. [Q6PDG8-1]
DR   ProteomicsDB; 290097; -. [Q6PDG8-2]
DR   Pumba; Q6PDG8; -.
DR   GeneID; 72825; -.
DR   KEGG; mmu:72825; -.
DR   UCSC; uc009rng.2; mouse. [Q6PDG8-1]
DR   UCSC; uc009rnh.2; mouse. [Q6PDG8-2]
DR   AGR; MGI:1920075; -.
DR   CTD; 84315; -.
DR   MGI; MGI:1920075; Mon1a.
DR   eggNOG; KOG0997; Eukaryota.
DR   InParanoid; Q6PDG8; -.
DR   OrthoDB; 73361at2759; -.
DR   PhylomeDB; Q6PDG8; -.
DR   TreeFam; TF314665; -.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 72825; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Mon1a; mouse.
DR   PRO; PR:Q6PDG8; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6PDG8; Protein.
DR   GO; GO:0035658; C:Mon1-Ccz1 complex; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:MGI.
DR   GO; GO:0009306; P:protein secretion; IMP:MGI.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IMP:MGI.
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; SAND PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13027:SF14; VACUOLAR FUSION PROTEIN MON1 HOMOLOG A; 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..556
FT                   /note="Vacuolar fusion protein MON1 homolog A"
FT                   /id="PRO_0000285763"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         61
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86VX9"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   VAR_SEQ         461
FT                   /note="S -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024913"
FT   VAR_SEQ         462..556
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024914"
FT   VARIANT         374
FT                   /note="N -> S (in strain: C57BL)"
FT                   /evidence="ECO:0000269|PubMed:17632513"
SQ   SEQUENCE   556 AA;  62131 MW;  78E1EA166530540F CRC64;
     MAADMQRKRS SECPEGTLAP SNGQSVERAE SPTPGLTQGT EPGAGQEGAM FVHTRSYEDL
     TELEDREASG DSPKECVGSP PPLATDMRQI SQDFSELSTQ LTGVARDLQE EMLPGSSEDW
     PEPQGAAGRG AATEPSQEGS TEGEEEDATE AWRLHQKHVF VLSEAGKPVY SRYGSEEALS
     STMGVMVALV SFLEADKNAI RSIHADGYKV VFVRRSPLVL VAVARTRQSA QELAQELLYI
     YYQILSLLTG AQLSHIFQQK QNYDLRRLLS GSERITDNLL QLMARDPSFL MGAARCLPLA
     AAVRDTVSAS LQQARARSLV FSILLAHNQL VALVRRKDQF LHPIDLHLLF NLISSSSSFR
     EGEAWTPVCL PKFNAAGFFH AHISYLEPDT DLCLLLISTD REDFFAVSDC RRRFQERLRK
     RGTHLALREA LRTPYYSVAQ VGIPDLRHFL YKSKSSGLFT SPEIEAPYSS EEEQERLLGL
     YQYLHSRAHN ASRPLKTIYY TGPNENLLAW VTGAFELYMC YSPLGTKASA VSAIHKLMRW
     IRKEEDRLFI LTPLTY
//