MARH7_MOUSE
ID MARH7_MOUSE Reviewed; 693 AA.
AC Q9WV66;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF7;
DE EC=2.3.2.27;
DE AltName: Full=Axotrophin;
DE AltName: Full=Membrane-associated RING finger protein 7;
DE AltName: Full=Membrane-associated RING-CH protein VII;
DE Short=MARCH-VII;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF7 {ECO:0000305};
GN Name=Marchf7; Synonyms=Axot, March7;
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], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15670816; DOI=10.1016/j.febslet.2004.12.027;
RA Metcalfe S.M., Muthukumarana P.A.D.S., Thompson H.L., Haendel M.A.,
RA Lyons G.E.;
RT "Leukaemia inhibitory factor (LIF) is functionally linked to axotrophin and
RT both LIF and axotrophin are linked to regulatory immune tolerance.";
RL FEBS Lett. 579:609-614(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance
CC the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfer the ubiquitin to targeted substrates (By similarity).
CC May be involved in T-cell proliferation by regulating LIF secretion
CC (PubMed:15670816). May play a role in lysosome homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:Q9H992,
CC ECO:0000269|PubMed:15670816}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Expressed in brain, thymus, muscle and kidney.
CC {ECO:0000269|PubMed:15670816}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in most tissues up to 15.5 dpc.
CC Thereafter, expressed at highest levels in the nervous system.
CC {ECO:0000269|PubMed:15670816}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- DISRUPTION PHENOTYPE: Mice have defects in formation of corpus callosum
CC and show degeneration of substantia gelatinosa lamina II axons in
CC adulthood. They have normal lymphoid development but show
CC hyperproliferation of T-cells in response to mitogens.
CC {ECO:0000269|PubMed:15670816}.
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DR EMBL; AF155739; AAD38411.1; -; mRNA.
DR EMBL; AK166666; BAE38928.1; -; mRNA.
DR EMBL; AK167246; BAE39367.1; -; mRNA.
DR EMBL; AK168555; BAE40429.1; -; mRNA.
DR EMBL; BC025029; AAH25029.1; -; mRNA.
DR CCDS; CCDS16057.1; -.
DR RefSeq; NP_065600.1; NM_020575.2.
DR AlphaFoldDB; Q9WV66; -.
DR SMR; Q9WV66; -.
DR STRING; 10090.ENSMUSP00000099809; -.
DR iPTMnet; Q9WV66; -.
DR PhosphoSitePlus; Q9WV66; -.
DR EPD; Q9WV66; -.
DR MaxQB; Q9WV66; -.
DR PaxDb; Q9WV66; -.
DR PeptideAtlas; Q9WV66; -.
DR PRIDE; Q9WV66; -.
DR ProteomicsDB; 295828; -.
DR Antibodypedia; 33721; 257 antibodies from 29 providers.
DR DNASU; 57438; -.
DR Ensembl; ENSMUST00000067542; ENSMUSP00000068961; ENSMUSG00000026977.
DR Ensembl; ENSMUST00000102747; ENSMUSP00000099808; ENSMUSG00000026977.
DR Ensembl; ENSMUST00000102748; ENSMUSP00000099809; ENSMUSG00000026977.
DR GeneID; 57438; -.
DR KEGG; mmu:57438; -.
DR UCSC; uc008jtx.1; mouse.
DR CTD; 64844; -.
DR MGI; MGI:1931053; Marchf7.
DR VEuPathDB; HostDB:ENSMUSG00000026977; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00530000063836; -.
DR HOGENOM; CLU_019830_0_0_1; -.
DR InParanoid; Q9WV66; -.
DR OMA; HIFRREA; -.
DR OrthoDB; 517602at2759; -.
DR PhylomeDB; Q9WV66; -.
DR TreeFam; TF330816; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57438; 1 hit in 41 CRISPR screens.
DR ChiTaRS; March7; mouse.
DR PRO; PR:Q9WV66; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WV66; protein.
DR Bgee; ENSMUSG00000026977; Expressed in pharyngeal arch 2 and 252 other tissues.
DR ExpressionAtlas; Q9WV66; baseline and differential.
DR Genevisible; Q9WV66; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IMP:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:1905524; P:negative regulation of protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0002643; P:regulation of tolerance induction; IMP:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..693
FT /note="E3 ubiquitin-protein ligase MARCHF7"
FT /id="PRO_0000274416"
FT ZN_FING 546..616
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 606
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 688
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
SQ SEQUENCE 693 AA; 76599 MW; 7082766DE39E4CED CRC64;
MESKPSRIPR RISVQPSGSL STRMVSGNRG TSLNDSYHSR DSSFRLDSEY QSASASACAS
PCQPAWYSES EIPQGARARA QTQQRDHDSK RPKLSCTNCA STSAGRNGGS GLNTVSDSSW
RHSQVPRSSS MVLGSFGTDL MRERRDLDRR RESSISNLMD YNHRSGDFTT SSYVQERVPS
SYSQGARPKE NAVSTLQLNS SSTNHQLPSD HQTVPSSRDS SRSSFRSHFS PRQSESFRNS
SHPAFSYFSS RNETPTISNS ERGSSQRPYR ESSDNEGRRT TRRLLSRIAS SMSSTFFSRR
SSQDSLNTRS LSSENYISPR TLTSQSRNNG TSSSSDVSEG RAAEASQGFR FLRRRWGLSS
LSQNHSSEPE AENFNQESEG RNSGPWLSSS LRNRCTPLFS RRRREGRDES SRMSTSDVPP
RSHIFRRDSN EVVHLEAQGD SLGAAANRPQ ASGASSSAAA GGSTPELPQG GRNPGLTGIL
PGSLFRFAVP PALGSNLADN VMITVDIIPS GWNSTDGKND KAKSAPSRDP EKLQKIKESL
LLEDSDDEEE GDLCRICQMA AASSSNLLIE PCKCTGSLQY VHQECMKKWL QAKINSGSSL
EAVTTCELCK EKLQLNLEDF DIHELHRAHA NEQAEYEFIS SGLYLVVLLH LCEQSFSDMM
GNTIEPSTRV RFINLARTLQ AHMEDLETSE DEF
