MARH7_PONAB
ID MARH7_PONAB Reviewed; 707 AA.
AC Q5R9W2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR859270; CAH91448.1; -; mRNA.
DR RefSeq; NP_001127420.1; NM_001133948.1.
DR AlphaFoldDB; Q5R9W2; -.
DR SMR; Q5R9W2; -.
DR STRING; 9601.ENSPPYP00000014365; -.
DR PRIDE; Q5R9W2; -.
DR GeneID; 100174490; -.
DR KEGG; pon:100174490; -.
DR CTD; 64844; -.
DR eggNOG; KOG1609; Eukaryota.
DR InParanoid; Q5R9W2; -.
DR OrthoDB; 517602at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
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: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:0050821; P:protein stabilization; ISS:UniProtKB.
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..707
FT /note="E3 ubiquitin-protein ligase MARCHF7"
FT /id="PRO_0000274417"
FT ZN_FING 544..614
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..473
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..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..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 448..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 607
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 317
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 686
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H992"
SQ SEQUENCE 707 AA; 78365 MW; 11ABEBF900382D57 CRC64;
MESKPSRIPR GISVQPSSSL SARMMSGSRG SSLNDTYHSR DSSFRLDSEY QSTSASASAS
PFQSAWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT TSAGRNVGNG LNTLSDSSWR
HSQVPRSSSM VLGSFGTDLM RERRDLERRT DSSISNLMDY SHRSGDFTTS SYVQDRVPSY
SQGARPKENS MSTLQLNTSS TNHQLPSEHQ TILSSRDSRS SLRSNFSSRE SESSRSNTQP
GFSYSSSRDE APIISNSERV VSSQRPFQES SDNEGRRTTR RLLSRIASSM SSTFFSRRSS
QDSLNTRSLS SENSYVSPRI LTASQSRSNV PSTSEVPDNR ASEASQGFRF LRRRWGLSSL
SHNHSSESDS ENFNQESESR NTGPWLSSSL RNRCTPLFSR RRREGRDESS RIPTSDTSSR
SHIFRRESNE VVHLEAQNDP LGAAANRPQA SAASSSATTG GSTSDSAQGG RNTGIAGILP
GSLFRFAVPP ALGSNLTDNV MITVDIIPSG WNSADGKSDK TKSAPSRDPE RLQKIKESLL
LEDSEEEEGD LCRICQMAAA SSSNLLIEPC KCTGSLQYVH QDCMKKWLQA KINSGSSLEA
VTTCELCKEK LELNLEDFDI HELHRAHANE QAEYEFISSG LYLVVLLHLC EQSFSDMMGN
TNEPSTRVRF INLARTLQAH MEDLETSEDD SEEDGDHNRT FDIAYFI
