ID   MARH4_HUMAN             Reviewed;         410 AA.
AC   Q9P2E8; Q4KMN7; Q86WR8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   07-NOV-2018, entry version 133.
DE   RecName: Full=E3 ubiquitin-protein ligase MARCH4;
DE            EC=2.3.2.27;
DE   AltName: Full=Membrane-associated RING finger protein 4;
DE   AltName: Full=Membrane-associated RING-CH protein IV;
DE            Short=MARCH-IV;
DE   AltName: Full=RING finger protein 174;
DE   AltName: Full=RING-type E3 ubiquitin transferase MARCH4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=MARCH4; Synonyms=KIAA1399, RNF174;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI.
RT   The complete sequences of 150 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver, and Pancreas;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14722266; DOI=10.1128/JVI.78.3.1109-1120.2004;
RA   Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
RT   "Downregulation of major histocompatibility complex class I by human
RT   ubiquitin ligases related to viral immune evasion proteins.";
RL   J. Virol. 78:1109-1120(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that may mediate
CC       ubiquitination of MHC-I and CD4, and promote their subsequent
CC       endocytosis and sorting to lysosomes via multivesicular bodies. E3
CC       ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
CC       conjugating enzyme in the form of a thioester and then directly
CC       transfer the ubiquitin to targeted substrates.
CC       {ECO:0000269|PubMed:14722266}.
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14722266}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and placenta.
CC       {ECO:0000269|PubMed:14722266}.
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC       ligase activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92637.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB037820; BAA92637.1; ALT_INIT; mRNA.
DR   EMBL; BC048793; AAH48793.1; -; mRNA.
DR   EMBL; BC098448; AAH98448.1; -; mRNA.
DR   CCDS; CCDS33376.1; -.
DR   RefSeq; NP_065865.1; NM_020814.2.
DR   UniGene; Hs.170388; -.
DR   ProteinModelPortal; Q9P2E8; -.
DR   SMR; Q9P2E8; -.
DR   BioGrid; 121627; 3.
DR   STRING; 9606.ENSP00000273067; -.
DR   iPTMnet; Q9P2E8; -.
DR   PhosphoSitePlus; Q9P2E8; -.
DR   BioMuta; MARCH4; -.
DR   DMDM; 59798475; -.
DR   PaxDb; Q9P2E8; -.
DR   PRIDE; Q9P2E8; -.
DR   ProteomicsDB; 83797; -.
DR   DNASU; 57574; -.
DR   Ensembl; ENST00000273067; ENSP00000273067; ENSG00000144583.
DR   GeneID; 57574; -.
DR   KEGG; hsa:57574; -.
DR   UCSC; uc002vgb.4; human.
DR   CTD; 57574; -.
DR   EuPathDB; HostDB:ENSG00000144583.4; -.
DR   GeneCards; MARCH4; -.
DR   HGNC; HGNC:29269; MARCH4.
DR   HPA; HPA014348; -.
DR   MIM; 608208; gene.
DR   neXtProt; NX_Q9P2E8; -.
DR   OpenTargets; ENSG00000144583; -.
DR   PharmGKB; PA134861849; -.
DR   eggNOG; KOG1609; Eukaryota.
DR   eggNOG; COG5183; LUCA.
DR   GeneTree; ENSGT00930000150936; -.
DR   HOGENOM; HOG000113484; -.
DR   HOVERGEN; HBG052412; -.
DR   InParanoid; Q9P2E8; -.
DR   KO; K10659; -.
DR   OMA; EDCYSLG; -.
DR   OrthoDB; EOG091G0JT5; -.
DR   PhylomeDB; Q9P2E8; -.
DR   TreeFam; TF319557; -.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; MARCH4; human.
DR   GenomeRNAi; 57574; -.
DR   PRO; PR:Q9P2E8; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000144583; Expressed in 54 organ(s), highest expression level in oocyte.
DR   CleanEx; HS_MARCH4; -.
DR   Genevisible; Q9P2E8; HS.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR033275; MARCH-like.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23012; PTHR23012; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Golgi apparatus; Membrane; Metal-binding;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    410       E3 ubiquitin-protein ligase MARCH4.
FT                                /FTId=PRO_0000055930.
FT   TRANSMEM    238    258       Helical. {ECO:0000255}.
FT   TRANSMEM    272    292       Helical. {ECO:0000255}.
FT   ZN_FING     155    215       RING-CH-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00623}.
FT   COMPBIAS     57    127       Pro-rich.
SQ   SEQUENCE   410 AA;  45528 MW;  BC812496FCCC2930 CRC64;
     MLMPLCGLLW WWWCCCSGWY CYGLCAPAPQ MLRHQGLLKC RCRMLFNDLK VFLLRRPPQA
     PLPMHGDPQP PGLAANNTLP ALGAGGWAGW RGPREVVGRE PPPVPPPPPL PPSSVEDDWG
     GPATEPPASL LSSASSDDFC KEKTEDRYSL GSSLDSGMRT PLCRICFQGP EQGELLSPCR
     CDGSVKCTHQ PCLIKWISER GCWSCELCYY KYHVIAISTK NPLQWQAISL TVIEKVQVAA
     AILGSLFLIA SISWLIWSTF SPSARWQRQD LLFQICYGMY GFMDVVCIGL IIHEGPSVYR
     IFKRWQAVNQ QWKVLNYDKT KDLEDQKAGG RTNPRTSSST QANIPSSEEE TAGTPAPEQG
     PAQAAGHPSG PLSHHHCAYT ILHILSHLRP HEQRSPPGSS RELVMRVTTV
//