MMS19_BOVIN
ID MMS19_BOVIN Reviewed; 1030 AA.
AC E1BP36; A6QPX1; F1MUW1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=MMS19 nucleotide excision repair protein homolog {ECO:0000250|UniProtKB:Q96T76};
DE AltName: Full=MMS19-like protein;
GN Name=MMS19 {ECO:0000250|UniProtKB:Q96T76};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key component of the cytosolic iron-sulfur protein assembly
CC (CIA) complex, a multiprotein complex that mediates the incorporation
CC of iron-sulfur cluster into apoproteins specifically involved in DNA
CC metabolism and genomic integrity. In the CIA complex, MMS19 acts as an
CC adapter between early-acting CIA components and a subset of cellular
CC target Fe/S proteins such as ERCC2/XPD, FANCJ and RTEL1, thereby
CC playing a key role in nucleotide excision repair (NER), homologous
CC recombination-mediated double-strand break DNA repair, DNA replication
CC and RNA polymerase II (POL II) transcription. As a CIA complex
CC component and in collaboration with CIAO1 and CIAO2, binds to and
CC facilitates the assembly of most cytosolic-nuclear Fe/S proteins. As
CC part of the mitotic spindle-associated MMXD complex, plays a role in
CC chromosome segregation, probably by facilitating iron-sulfur cluster
CC assembly into ERCC2/XPD. Together with CIAO2, facilitates the transfer
CC of Fe-S clusters to the motor protein KIF4A, which ensures proper
CC localization of KIF4A to mitotic machinery components to promote the
CC progression of mitosis. Indirectly acts as a transcriptional
CC coactivator of estrogen receptor (ER), via its role in iron-sulfur
CC insertion into some component of the TFIIH-machinery.
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- SUBUNIT: Component of the CIA complex. In the CIA complex, interacts
CC directly with CIAO2B and CIAO3. Component of the MMXD complex, composed
CC of CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5. Interacts with CIAO2B; the
CC interaction is direct. Interacts with ERCC2/XPD; the interaction is
CC direct. Interacts with ERCC3/XPB and NCOA3/RAC3. Interacts with RTEL1;
CC the interaction mediates the association of RTEL1 with the CIA complex.
CC Interacts with BRIP1. Interacts with KIF4A; the interaction facilitates
CC the transfer of Fe-S clusters to KIF4A to ensure proper localization of
CC KIF4A to the mitotic machinery components. Interacts with CCDC117; the
CC interaction is indirect (By similarity).
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96T76}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96T76}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E1BP36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E1BP36-2; Sequence=VSP_044195, VSP_044196;
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:Q96T76}.
CC -!- SIMILARITY: Belongs to the MET18/MMS19 family. {ECO:0000305}.
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DR EMBL; DAAA02058916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03054038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03054039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC149532; AAI49533.1; -; mRNA.
DR RefSeq; NP_001095627.1; NM_001102157.2.
DR RefSeq; XP_005225615.1; XM_005225558.3. [E1BP36-1]
DR AlphaFoldDB; E1BP36; -.
DR SMR; E1BP36; -.
DR STRING; 9913.ENSBTAP00000053458; -.
DR PaxDb; E1BP36; -.
DR PRIDE; E1BP36; -.
DR Ensembl; ENSBTAT00000061179; ENSBTAP00000053458; ENSBTAG00000012704. [E1BP36-1]
DR GeneID; 533499; -.
DR KEGG; bta:533499; -.
DR CTD; 64210; -.
DR VEuPathDB; HostDB:ENSBTAG00000012704; -.
DR eggNOG; KOG1967; Eukaryota.
DR GeneTree; ENSGT00390000015583; -.
DR HOGENOM; CLU_005943_2_0_1; -.
DR InParanoid; E1BP36; -.
DR OMA; FSFMPEF; -.
DR OrthoDB; 944339at2759; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000012704; Expressed in biceps femoris and 107 other tissues.
DR ExpressionAtlas; E1BP36; baseline and differential.
DR GO; GO:0097361; C:CIA complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071817; C:MMXD complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006259; P:DNA metabolic process; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039920; MET18/MMS19.
DR InterPro; IPR024687; MMS19_C.
DR InterPro; IPR029240; MMS19_N.
DR PANTHER; PTHR12891; PTHR12891; 1.
DR Pfam; PF12460; MMS19_C; 1.
DR Pfam; PF14500; MMS19_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Alternative splicing; Chromosome partition;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT CHAIN 2..1030
FT /note="MMS19 nucleotide excision repair protein homolog"
FT /id="PRO_0000419480"
FT REPEAT 866..904
FT /note="HEAT 1"
FT REPEAT 908..946
FT /note="HEAT 2"
FT REPEAT 949..987
FT /note="HEAT 3"
FT REPEAT 990..1028
FT /note="HEAT 4"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T76"
FT VAR_SEQ 502..503
FT /note="CR -> W (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044195"
FT VAR_SEQ 730..1030
FT /note="EIPQLNRLMGELLELSCCQSCPFSSTAAAKCFAGLLNKHPAGQQLDEFLQLA
FT VDKVEAGLSSGPCRSQAFTLLLWVTKALVLRYHPLSSCLTERLMGLLSDPELGPAAADG
FT FSLLMSDCTDVLTRAGHAEVRIMFRQRFFTDNVPALVRGFHAAPQDVKPNYLKGLSHVL
FT NRLPKPVLLPELPTLLSLLLEALSCPDSVVQLSTLSCLQPLLLEAPQVMSLHVDTLITK
FT FLNLSASPSMAVRIAALQCMHALTRLPTPVLLPYKPQVIRALAKPLDDKKRLVRKEAVS
FT ARGEWFLLGSPGS -> FYRWKSHS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044196"
FT CONFLICT 426
FT /note="K -> E (in Ref. 3; AAI49533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1030 AA; 113112 MW; B21A056390F11C2B CRC64;
MAAAAALEAV APLGTLWGLV QDFVMGQQEG PADQVAADVK SGSYTVLQVV EALGSSLENP
EPRTRARGIQ LLSQVLLQCH SLLLEKEVVH LILFYENRLK DHHLVIPSVL QGLRALSLCV
TLPPGLAVSV LKAIFQEVHV QSLPQVDRHT VYSIITNFMR AREEELKGLG ADFTFGFIQV
MDGEKDPRNL LVAFHIVYDL ISRDYSLGPF VEELFEVTSC YFPIDFTPPP NDPHGIQRED
LILSLRAVLA STPRFAEFLL PLLIEKVDSE ILSAKLDSLQ TLNACCAVYG QKELKDFLPS
LWASIRREVF QTASERVEAE GLAALNSLTA CLSRSVLRAD AEDLLDSFLS NILQDCRHHL
CEPDMKLVWP SAKLLQAAAG ASARACDHVT SNVLPLLLEQ FHKHSQSNQR RTILEMILGF
LKLQQKWSYE DKDERPLSGF KDQLCSLMFM ALTDPNTQLQ LVGIRTLTVL GAQPDLLSSG
DLELAVGHLY RLSFLEEDSQ SCRVAALEAS GTLATLYPMA FSSHLVPRLA EDLCTEESDL
ARADGPTRCS RHPRCLQALS AISTHPSIVK ETLPLLLQHL CQMNRGSVSP GTSEVIAVCQ
SLQQVAENCQ RDPESCWYFH QTAVPCLLAL VVQASAPEKE HSVLKKVLLE DEVLATMASV
IATATTHLSP DLASQSVAHI VPLFLDGNIS FLPENSFSGR FQPFQDGSSG QRRLVALLMA
FVCSLPRNVE IPQLNRLMGE LLELSCCQSC PFSSTAAAKC FAGLLNKHPA GQQLDEFLQL
AVDKVEAGLS SGPCRSQAFT LLLWVTKALV LRYHPLSSCL TERLMGLLSD PELGPAAADG
FSLLMSDCTD VLTRAGHAEV RIMFRQRFFT DNVPALVRGF HAAPQDVKPN YLKGLSHVLN
RLPKPVLLPE LPTLLSLLLE ALSCPDSVVQ LSTLSCLQPL LLEAPQVMSL HVDTLITKFL
NLSASPSMAV RIAALQCMHA LTRLPTPVLL PYKPQVIRAL AKPLDDKKRL VRKEAVSARG
EWFLLGSPGS
