ID   MARH9_MOUSE             Reviewed;         348 AA.
AC   Q3TZ87; Q8VCL1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=E3 ubiquitin-protein ligase MARCHF9;
DE            EC=2.3.2.27;
DE   AltName: Full=Membrane-associated RING finger protein 9;
DE   AltName: Full=Membrane-associated RING-CH protein IX;
DE            Short=MARCH-IX;
DE   AltName: Full=RING-type E3 ubiquitin transferase MARCHF9 {ECO:0000305};
GN   Name=Marchf9; Synonyms=March9;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-348.
RC   STRAIN=FVB/N; TISSUE=Colon;
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 that may mediate ubiquitination
CC       of MHC-I, CD4 and ICAM1, and promote their subsequent endocytosis and
CC       sorting to lysosomes via multivesicular bodies. 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:0000250|UniProtKB:Q86YJ5}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86YJ5}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q86YJ5}; Multi-pass membrane protein
CC       {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q86YJ5}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC       activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK158026; BAE34323.1; -; mRNA.
DR   EMBL; BC019560; AAH19560.1; ALT_INIT; mRNA.
DR   CCDS; CCDS24225.1; -.
DR   RefSeq; NP_001028434.1; NM_001033262.2.
DR   AlphaFoldDB; Q3TZ87; -.
DR   STRING; 10090.ENSMUSP00000041581; -.
DR   PhosphoSitePlus; Q3TZ87; -.
DR   PaxDb; 10090-ENSMUSP00000041581; -.
DR   ProteomicsDB; 295829; -.
DR   Antibodypedia; 28932; 195 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000040307.6; ENSMUSP00000041581.6; ENSMUSG00000040502.6.
DR   GeneID; 216438; -.
DR   KEGG; mmu:216438; -.
DR   UCSC; uc007hhu.1; mouse.
DR   AGR; MGI:2446144; -.
DR   MGI; MGI:2446144; Marchf9.
DR   VEuPathDB; HostDB:ENSMUSG00000040502; -.
DR   eggNOG; KOG1609; Eukaryota.
DR   GeneTree; ENSGT00940000158208; -.
DR   HOGENOM; CLU_045217_0_0_1; -.
DR   InParanoid; Q3TZ87; -.
DR   OMA; HCRYTIL; -.
DR   OrthoDB; 1342875at2759; -.
DR   PhylomeDB; Q3TZ87; -.
DR   TreeFam; TF319557; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 216438; 0 hits in 46 CRISPR screens.
DR   PRO; PR:Q3TZ87; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q3TZ87; Protein.
DR   Bgee; ENSMUSG00000040502; Expressed in cortical plate and 164 other cell types or tissues.
DR   Genevisible; Q3TZ87; MM.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16811; RING_CH-C4HC3_MARCH4_9; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046356; MARCHF4/9/11.
DR   InterPro; IPR047904; MARCHF9_RING_CH-C4HC3.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR   PANTHER; PTHR46053:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF9; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Lysosome; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..348
FT                   /note="E3 ubiquitin-protein ligase MARCHF9"
FT                   /id="PRO_0000274283"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         102..162
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   REGION          48..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ   SEQUENCE   348 AA;  37888 MW;  0062DB303278CD17 CRC64;
     MLKSRLRMFL NELKLLVLTG GGRPRAEPQP RGGGGGGCGW APFAGCSARD GDGDEEEYYG
     SEPRARGLAG DKEPRAGPPP PPAPPPPPPG ALDALSLSSS LDSGLRTPQC RICFQGPEQG
     ELLSPCRCDG SVRCTHQPCL IRWISERGSW SCELCYFKYQ VLAISTKNPL QWQAISLTVI
     EKVQIAAIVL GSLFLVASIS WLIWSSLSPS AKWQRQDLLF QICYGMYGFM DVVCIGLIVH
     EGSSVYRIFK RWQAVNQQWK VLNYDKTKDV GGDTGGGAAG KPGPRTSRTS PPAGAPTRPP
     AAQRMRMRTL LPQRCGYTIL HLLGQLRPPD ARSSSHSGRE VVMRVTTV
//