MARH7_RAT
ID MARH7_RAT Reviewed; 692 AA.
AC Q5XI50;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF7;
DE EC=2.3.2.27;
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=March7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 (By
CC similarity). May play a role in lysosome homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:Q9H992, ECO:0000250|UniProtKB:Q9WV66}.
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 -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; BC083842; AAH83842.1; -; mRNA.
DR RefSeq; NP_001012087.1; NM_001012087.1.
DR RefSeq; XP_017447174.1; XM_017591685.1.
DR AlphaFoldDB; Q5XI50; -.
DR SMR; Q5XI50; -.
DR STRING; 10116.ENSRNOP00000008464; -.
DR iPTMnet; Q5XI50; -.
DR PhosphoSitePlus; Q5XI50; -.
DR PaxDb; Q5XI50; -.
DR PRIDE; Q5XI50; -.
DR Ensembl; ENSRNOT00000109892; ENSRNOP00000092770; ENSRNOG00000006241.
DR GeneID; 311059; -.
DR KEGG; rno:311059; -.
DR UCSC; RGD:1308993; rat.
DR CTD; 64844; -.
DR RGD; 1308993; March7.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00530000063836; -.
DR InParanoid; Q5XI50; -.
DR OMA; HIFRREA; -.
DR OrthoDB; 517602at2759; -.
DR PhylomeDB; Q5XI50; -.
DR TreeFam; TF330816; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5XI50; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006241; Expressed in testis and 18 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:RGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:RGD.
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; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0002643; P:regulation of tolerance induction; ISO:RGD.
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..692
FT /note="E3 ubiquitin-protein ligase MARCHF7"
FT /id="PRO_0000274418"
FT ZN_FING 545..615
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..532
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 46..80
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 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..271
FT /note="Polar 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 360..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 556
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 608
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 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
SQ SEQUENCE 692 AA; 76351 MW; D31187065BB3CFAC CRC64;
MESKPSRIPR RISVQPSGSL SARMVSGNRG TSLNDSYHSR DSSFRLDSEY QSASASASAS
PYQSTWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT STSAGRNIGS GLNTLSDSSW
RPGQVPRSSS MVLGSFGTDL MRERRDLERR RDSSISSLMD YSHRSGDFTA PAYVQERVPS
SYSQGARPKE NAANTLQLNS STNHQLPSEH QTVPSSRDSS RSSFRSHFSP RQSESFRNSS
HPAFSYLSSR NETPTISSSE RAGSSQRPFQ ESSDNEGRRT TRRLLSRIAS SMSSTFFSRR
SSQDSLNTRS LSSENYISPR TLTSQSRNNG ASSSEVNDGR ASEASQGFRF LRRRWGLSSL
SQNHSSEPDA ENFNQESEGR NTGPWLSSSL RNRCTPLFSR RRREGRDESS RISPSDVPPR
SHLFRRESNE VVHLEAQGDS LGAAASRPQA SGASGNASAS GSTPDLPQGG RNTGIAGILP
GSLFRFAVPP ALGSNLTDNV TITVDIIPSG WSSADGKSEK AKSAPSRDPE KLQKIKESLL
LEDSDEEEEG DLCRICQMAA ASSSNLLIEP CKCTGSLQYV HQECMKKWLQ AKINSGSSLE
AVTTCELCKE KLQLNLEDFD IHELHRAHAN EQAEYEFISS GLYLVVLLHL CEQSFSDMMG
NTIEPSTRVR FINLARTLQA HMEDLETSED EF
