MARHA_RAT
ID MARHA_RAT Reviewed; 790 AA.
AC Q5XIV2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable E3 ubiquitin-protein ligase MARCHF10;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 10;
DE AltName: Full=Membrane-associated RING-CH protein X;
DE Short=MARCH-X;
DE AltName: Full=RING finger protein 190;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF10 {ECO:0000305};
GN Name=Marchf10; Synonyms=March10, Rnf190;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases
CC accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of
CC a thioester and then directly transfer the ubiquitin to targeted
CC substrates. {ECO:0000305}.
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; BC083567; AAH83567.1; -; mRNA.
DR RefSeq; NP_001013995.1; NM_001013973.1.
DR RefSeq; XP_017452826.1; XM_017597337.1.
DR RefSeq; XP_017452827.1; XM_017597338.1.
DR AlphaFoldDB; Q5XIV2; -.
DR SMR; Q5XIV2; -.
DR STRING; 10116.ENSRNOP00000009316; -.
DR iPTMnet; Q5XIV2; -.
DR PhosphoSitePlus; Q5XIV2; -.
DR PaxDb; Q5XIV2; -.
DR PRIDE; Q5XIV2; -.
DR Ensembl; ENSRNOT00000009316; ENSRNOP00000009316; ENSRNOG00000007084.
DR GeneID; 303596; -.
DR KEGG; rno:303596; -.
DR UCSC; RGD:1311692; rat.
DR CTD; 162333; -.
DR RGD; 1311692; March10.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00530000063836; -.
DR HOGENOM; CLU_021725_0_0_1; -.
DR InParanoid; Q5XIV2; -.
DR OMA; HDYERDW; -.
DR OrthoDB; 517602at2759; -.
DR PhylomeDB; Q5XIV2; -.
DR TreeFam; TF330816; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5XIV2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007084; Expressed in testis and 9 other tissues.
DR ExpressionAtlas; Q5XIV2; baseline and differential.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16813; RING_CH-C4HC3_MARCH10; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042583; MARCH10_RING_CH-C4HC3.
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 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..790
FT /note="Probable E3 ubiquitin-protein ligase MARCHF10"
FT /id="PRO_0000261627"
FT ZN_FING 633..703
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 33..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..308
FT /evidence="ECO:0000255"
FT COMPBIAS 33..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 644
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 696
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 790 AA; 87886 MW; E5DAE696C792EA0D CRC64;
MLHEARDRQK FVSDVQYLRD MQHKVDSEYQ ACLKRQEHKK EPNEKKQEQL WGKDTSDRSR
FSSGSSCKQS SGEEDSLSEA RLATKAPTAK CEPKLPAIDQ TSVKQKHKGT MTLKKPEKVS
PSKPSAVAQA TKILSRKRRP NLGRLTVSPE MHSPRLSGER SRQKAQLSTK TSGLLGADPV
VQQDSLLSAN EMKLKRPARE KRNLAPSSQL VRVAGKAPLE RQKKGDPSAR PQNEPHTALS
QTFQPMSGSQ VLTESSVPPF LPATVVGPRR APFRFHDEDF YSALSLNNEQ ENYDTEEETR
TEEELLLAGM RSPPSYKRSR FLGTSAAQNR NVEENAENLR GNSLRRSEPN PGSPRKTSVT
EPTTKQSSPG QRMLQDTRLP RELAKDNPSG DQDEKTPVPG DAKSDGVTQV SAEDVSNNCA
VEDRSAVHNC ERDWQRYLSG SRNSFDCLLS GRPTAPRASV NPSYNAHGSL FHSAVIDDIP
ASLSVSSILV PSAELEENLR FNVRRPLSPI RNRNPSAASE SHSEDTQGEE ERASTSQAQE
SPLLSDLPNP QSSMALGDSP SSPTRRHLQG HFYMPGSLQE NIPFTFFAVS DFASQNDNGT
SVRVSGVMDE KATEIKADPE KLRKLQESLL EEDSEEEGDL CRICQIAGGS PANPLLEPCG
CVGSLQFVHQ ECLKKWLKVK ITSGADLSTV KTCEMCKQGL LVDLDDFNMT EFYHKHQQSR
AQSELMNSGL YLVLLLHLYE QRFAELMTLN YRRASRERMS RNYPQPRPEE SESSESGDGN
ESNVYPGRVI
