ID G7NNA5_MACMU Unreviewed; 246 AA.
AC G7NNA5; A0A5F7ZPE6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF2 {ECO:0000256|ARBA:ARBA00040156};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Membrane-associated RING finger protein 2 {ECO:0000256|ARBA:ARBA00043183};
DE AltName: Full=Membrane-associated RING-CH protein II {ECO:0000256|ARBA:ARBA00042437};
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF2 {ECO:0000256|ARBA:ARBA00043232};
GN Name=MARCHF2 {ECO:0000313|Ensembl:ENSMMUP00000066495.1,
GN ECO:0000313|VGNC:VGNC:112133};
GN Synonyms=MARCH2 {ECO:0000313|EMBL:AFE64354.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000066495.1, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|EMBL:AFE64354.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE64354.1}, Testis
RC {ECO:0000313|EMBL:AFI34829.1}, and Thymus
RC {ECO:0000313|EMBL:AFH27406.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000066495.1}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000066495.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JU320598; AFE64354.1; -; mRNA.
DR EMBL; JU470602; AFH27406.1; -; mRNA.
DR EMBL; JV044758; AFI34829.1; -; mRNA.
DR RefSeq; XP_014978214.1; XM_015122728.1.
DR Ensembl; ENSMMUT00000085953.1; ENSMMUP00000078403.1; ENSMMUG00000043959.2.
DR Ensembl; ENSMMUT00000090345.1; ENSMMUP00000068861.1; ENSMMUG00000043959.2.
DR Ensembl; ENSMMUT00000108975.1; ENSMMUP00000066495.1; ENSMMUG00000043959.2.
DR GeneID; 711857; -.
DR KEGG; mcc:711857; -.
DR CTD; 51257; -.
DR VEuPathDB; HostDB:ENSMMUG00000043959; -.
DR VGNC; VGNC:112133; MARCHF2.
DR GeneTree; ENSGT00940000158995; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000006718; Chromosome 19.
DR Bgee; ENSMMUG00000043959; Expressed in superior frontal gyrus and 22 other cell types or tissues.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16808; RING_CH-C4HC3_MARCH2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46065; E3 UBIQUITIN-PROTEIN LIGASE MARCH 2/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR46065:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF2; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 142..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..116
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 64..110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 220..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 26985 MW; 38D877D55211CB44 CRC64;
MTTGDCCHLP GSLCDCSGSP AFSKVVEATG LGPPQYVAQV TSRDGRLLST VIRALDTPSD
GPFCRICHEG ANGECLLSPC GCTGTLGAVH KSCLEKWLSS SNTSYCELCH TEFAVEKRPR
PLTEWLKDPG PRTEKRTLCC DMVCFLFITP LAAISGWLCL RGAQDHLRLH SQLEAVGLIA
LTIALFTIYV LWTLVSFRYH CQLYSEWRKT NQKVRLKIRE ADSSEGPQHS PLAAGLLKKV
AEETPV
//
