MON2_MOUSE
ID MON2_MOUSE Reviewed; 1715 AA.
AC Q80TL7; Q3TRE3; Q8BTA8; Q8K4V3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein MON2 homolog;
DE AltName: Full=Protein SF21;
GN Name=Mon2; Synonyms=Kiaa1040, Sf21;
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 [MRNA] (ISOFORM 2).
RA Inagaki S.;
RT "A novel mouse gene showing weak similarity to C. elegans F11A10.4
RT hypothetical protein.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 891-1715 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
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 [4]
RP IDENTIFICATION.
RX PubMed=16219684; DOI=10.1242/jcs.02599;
RA Efe J.A., Plattner F., Hulo N., Kressler D., Emr S.D., Deloche O.;
RT "Yeast Mon2p is a highly conserved protein that functions in the cytoplasm-
RT to-vacuole transport pathway and is required for Golgi homeostasis.";
RL J. Cell Sci. 118:4751-4764(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Plays a role in regulating membrane trafficking of cargo
CC proteins. Together with ATP9A and DOP1B, regulates SNX3 retromer-
CC mediated endosomal sorting of WLS away from lysosomal degradation.
CC {ECO:0000250|UniProtKB:Q7Z3U7}.
CC -!- SUBUNIT: Homooligomer. Heterotrimer with ATP9A and DOP1B; this
CC interaction is retromer-independent. Interacts with SNX3.
CC {ECO:0000250|UniProtKB:Q7Z3U7}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q7Z3U7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TL7-2; Sequence=VSP_027394, VSP_027395;
CC -!- SIMILARITY: Belongs to the MON2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25345.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65707.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB014059; BAC11706.1; -; mRNA.
DR EMBL; AK011826; BAC25345.1; ALT_FRAME; mRNA.
DR EMBL; AK122425; BAC65707.1; ALT_INIT; mRNA.
DR EMBL; AK162859; BAE37087.1; -; mRNA.
DR CCDS; CCDS24216.1; -. [Q80TL7-2]
DR CCDS; CCDS48707.1; -. [Q80TL7-1]
DR RefSeq; NP_001156496.1; NM_001163024.1. [Q80TL7-1]
DR RefSeq; NP_700444.2; NM_153395.2. [Q80TL7-2]
DR AlphaFoldDB; Q80TL7; -.
DR BioGRID; 211921; 2.
DR IntAct; Q80TL7; 1.
DR MINT; Q80TL7; -.
DR STRING; 10090.ENSMUSP00000073462; -.
DR iPTMnet; Q80TL7; -.
DR PhosphoSitePlus; Q80TL7; -.
DR SwissPalm; Q80TL7; -.
DR EPD; Q80TL7; -.
DR jPOST; Q80TL7; -.
DR MaxQB; Q80TL7; -.
DR PaxDb; Q80TL7; -.
DR PeptideAtlas; Q80TL7; -.
DR PRIDE; Q80TL7; -.
DR ProteomicsDB; 291379; -. [Q80TL7-1]
DR ProteomicsDB; 291380; -. [Q80TL7-2]
DR Antibodypedia; 51455; 31 antibodies from 12 providers.
DR Ensembl; ENSMUST00000037557; ENSMUSP00000037568; ENSMUSG00000034602. [Q80TL7-2]
DR Ensembl; ENSMUST00000073792; ENSMUSP00000073462; ENSMUSG00000034602. [Q80TL7-1]
DR GeneID; 67074; -.
DR KEGG; mmu:67074; -.
DR UCSC; uc007hgj.2; mouse. [Q80TL7-1]
DR UCSC; uc007hgk.2; mouse. [Q80TL7-2]
DR CTD; 23041; -.
DR MGI; MGI:1914324; Mon2.
DR VEuPathDB; HostDB:ENSMUSG00000034602; -.
DR eggNOG; KOG0929; Eukaryota.
DR eggNOG; KOG1848; Eukaryota.
DR GeneTree; ENSGT00390000013286; -.
DR HOGENOM; CLU_001169_2_0_1; -.
DR InParanoid; Q80TL7; -.
DR OMA; DETIDCQ; -.
DR OrthoDB; 411011at2759; -.
DR PhylomeDB; Q80TL7; -.
DR TreeFam; TF314287; -.
DR BioGRID-ORCS; 67074; 15 hits in 76 CRISPR screens.
DR ChiTaRS; Mon2; mouse.
DR PRO; PR:Q80TL7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80TL7; protein.
DR Bgee; ENSMUSG00000034602; Expressed in humerus cartilage element and 230 other tissues.
DR ExpressionAtlas; Q80TL7; baseline and differential.
DR Genevisible; Q80TL7; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR026829; Mon2-like.
DR InterPro; IPR032817; Mon2_C.
DR InterPro; IPR015403; Sec7_C.
DR InterPro; IPR032691; Sec7_N.
DR PANTHER; PTHR10663:SF333; PTHR10663:SF333; 1.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF09324; DUF1981; 1.
DR Pfam; PF16206; Mon2_C; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3U7"
FT CHAIN 2..1715
FT /note="Protein MON2 homolog"
FT /id="PRO_0000297903"
FT REGION 506..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3U7"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3U7"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 820
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_027394"
FT VAR_SEQ 1391..1396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_027395"
FT CONFLICT 1065
FT /note="V -> I (in Ref. 1; BAC11706)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126
FT /note="T -> N (in Ref. 3; BAE37087)"
FT /evidence="ECO:0000305"
FT CONFLICT 1195
FT /note="L -> F (in Ref. 1; BAC11706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1715 AA; 189078 MW; 0D4761F77C7A6490 CRC64;
MSCTNSPEAV KKLLENMQSD LRALSLECKK KFPPVKEAAE SGIIKVKTIA ARNTEILAAL
KENSSEVVQP FLMGCGTKEP KITQLCLAAI QRLMSHEVVS ETAAGNIINM LWQLMENSLE
ELKLLQTVLV LLTTNTVVHD EALSKAIVLC FRLHFTKDNI TNNTAAATVR QVVTVVFERM
VAEDDRHRDI EPPVPIQGNS NRRSVSTLRP CAKDAYMLFQ DLCQLVNADA PYWLVGMTEM
TRTFGLELLE SVLNDFPQVF LQHQEFSFLL KERVCPLVIK LFSPNIKFRQ GSSTSSSPAP
VEKPYFPICM RLLRVVSVLI KQFYSLLVTE CEIFLSLLVK FLDSDKPQWL RAVAVESIHR
LCVQPQLLRS FCQSYDMKQH STKVFRDIVN ALGSFIQSLF LVPPTGNPAT ANQAGNNNAG
GPASAPANSG VVGVGGGVTL LPAFEYRGAW IPILTVTVQG SAKATYLEML DKVEPPTIPE
GYAMSVAFHC LLDLVRGITT MIEGELGEVE AEGPSVTEGA SSQSSERRDE QAASDPMDQE
TVSRAVWEEM VSACWCGLLA ALSLLLDAST DEAATENILK AELTMAALCG RLGLVTSRDA
FITAICKGSL PPHYALTVLN ATTAATLSNK SYSIQGQSVM MISPSSESHQ QVVAVGQPLA
VQPQGTVMLT SKNIQCMRTL LNLAHCHGAV LGTSWQLVLA TLQHLVWILG LKPSSGGALK
PGRAVEGPST VLTTAVMTDL PVISNILSRL FESSQYLDDV SLHHLINALC SLSLEAMDMA
YGNNKEPSLF AVAKLLETGL VNMHRIEILW RPLTGHLLEK VCQHPNSRMR EWGAEALTSL
IRAGLTFSHE PPLPQNQRLQ LLLLNPLKEM SNINHPDIRL KQLECVLQIL QSQGDSLGPG
WPLVLGVMGA IRNDQGESLI RTAFQCLQLV VTDFLPTMPC SCLQIVVDVA GSFGLHNQEL
NISLTSIGLL WNISDYFFQR GETIEKELNK EEAAQQKQAE EKGVSLNRPF HPAPPFDCLW
LCLYAKLGEL CVDPRPAVRK SAGQTLFSTI GAHGTLLQHS TWHTVIWKVL FHLLDRVRES
STTADKEKIE SGGGNILIHH SRDTAEKQWA ETWVLTLAGV ARIFNTRRYL LQPLGDFSRA
WDVLLDHIQS AALSKNNEVS LAALKSFQEI LQIVSPVRDS EKPEPPAVSV PVPVLLGNLS
GPGLSRPFVR TDSIGEKLGR CGSETPVVTD ELEDLKLWWA AWNTWHRTGS ESTEPPSSVD
ELTFIPSQPF LTALVQIFPA LYQHIKAGFS MADLQKLGVI LHSAVSVPIS SDASPFILPS
YTEAVLTSLQ EAVLTALDVL QKAICVGPEN MQIMYPAIFD QLLAFVEFSC KPPQYGQLET
KHIANAKYNQ IQLFAPAEWV ALNYVPFAER SLEVVVDLYQ KTACHKAVVN EKVLQNIIKT
LRVPLSLKYS CPSESTWKLA VASLLKVLSI GLPVARQHAS SGKFDSMWPE LASTLEDFLF
TKSIPPDNLS IQEFQRNESI DVEVVQLISA EILPYANLIP KAFVGQMMTM LNKGSIHSQP
CSFTEAEIDI RLREEFSKMC FETLLQFSFS NKVTTPQEGY ISRMALSVLL KRSQDVLHRY
IEDERLSGKC PLPRQQVTEI IFVLKAVSTL IDSLKKTQPE NVDGNTWSQV IALYPTLVEC
ITCSSSDVGS ALKEALAPFK DFMQPPASRV QNGES
