MAC1_CAEEL
ID MAC1_CAEEL Reviewed; 813 AA.
AC Q9NAG4; Q9U8K0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein mac-1 {ECO:0000305};
DE AltName: Full=Member of AAA family that binds ced-4 {ECO:0000303|PubMed:10101135};
GN Name=mac-1 {ECO:0000303|PubMed:10101135};
GN ORFNames=Y48C3A.7 {ECO:0000312|WormBase:Y48C3A.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A CED-4/ CED-3 AND
RP CED-4/CED-9 COMPLEX, INTERACTION WITH CED-4, AND DISRUPTION PHENOTYPE.
RX PubMed=10101135; DOI=10.1242/dev.126.9.2021;
RA Wu D., Chen P.J., Chen S., Hu Y., Nunez G., Ellis R.E.;
RT "C. elegans MAC-1, an essential member of the AAA family of ATPases, can
RT bind CED-4 and prevent cell death.";
RL Development 126:2021-2031(1999).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Probably together with ced-9, plays a modest role in
CC preventing ced-4 and caspase ced-3-mediated apoptosis.
CC {ECO:0000269|PubMed:10101135}.
CC -!- SUBUNIT: Found in a complex composed of ced-3, ced-4 and mac-1 or of
CC ced-9, ced-4 and mac-1. Within the complex, interacts with ced-4.
CC {ECO:0000269|PubMed:10101135}.
CC -!- INTERACTION:
CC Q9NAG4; P30429-2: ced-4; NbExp=8; IntAct=EBI-2005767, EBI-536271;
CC Q9NAG4; Q9U2Q9: gsk-3; NbExp=3; IntAct=EBI-2005767, EBI-330089;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at the
CC L2-L3 larval stages with few adults reaching adulthood. Abnormal
CC presence of vacuoles in the intestine with some intestinal sections
CC almost completely degraded. RNAi-mediated knockdown in a ced-3 (n718)
CC or ced-4 (n1416) mutant background causes a similar arrest at the L2-L3
CC larval stages. {ECO:0000269|PubMed:10101135}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF059715; AAF05624.1; -; mRNA.
DR EMBL; BX284602; CAB55106.2; -; Genomic_DNA.
DR PIR; T31591; T31591.
DR RefSeq; NP_496814.1; NM_064413.7.
DR AlphaFoldDB; Q9NAG4; -.
DR SMR; Q9NAG4; -.
DR ComplexPortal; CPX-1358; ced-3-ced-4-mac-1 complex.
DR ComplexPortal; CPX-1359; ced-4-ced-9-mac-1 complex.
DR IntAct; Q9NAG4; 4.
DR STRING; 6239.Y48C3A.7; -.
DR EPD; Q9NAG4; -.
DR PaxDb; Q9NAG4; -.
DR PeptideAtlas; Q9NAG4; -.
DR EnsemblMetazoa; Y48C3A.7.1; Y48C3A.7.1; WBGene00003119.
DR GeneID; 174974; -.
DR KEGG; cel:CELE_Y48C3A.7; -.
DR UCSC; Y48C3A.7; c. elegans.
DR CTD; 174974; -.
DR WormBase; Y48C3A.7; CE28132; WBGene00003119; mac-1.
DR eggNOG; KOG0733; Eukaryota.
DR GeneTree; ENSGT00570000079239; -.
DR HOGENOM; CLU_000688_8_3_1; -.
DR InParanoid; Q9NAG4; -.
DR OMA; RQVFMRA; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; Q9NAG4; -.
DR SignaLink; Q9NAG4; -.
DR PRO; PR:Q9NAG4; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003119; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0008303; C:caspase complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:1990275; F:preribosome binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019915; P:lipid storage; IMP:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IMP:ComplexPortal.
DR GO; GO:0061063; P:positive regulation of nematode larval development; IMP:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR Gene3D; 1.10.10.2010; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR038100; NLV2_N_sf.
DR InterPro; IPR031996; NVL2_nucleolin-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF16725; Nucleolin_bd; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Coiled coil; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..813
FT /note="Protein mac-1"
FT /id="PRO_0000441159"
FT REGION 97..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..89
FT /evidence="ECO:0000255"
FT COILED 122..152
FT /evidence="ECO:0000255"
FT COMPBIAS 152..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 575..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15381"
FT CONFLICT 386..394
FT /note="GLRRAGRFE -> RLRRTGRFQ (in Ref. 1; AAF05624)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="I -> F (in Ref. 1; AAF05624)"
FT /evidence="ECO:0000305"
FT CONFLICT 748..753
FT /note="ALIHES -> VFIHEL (in Ref. 1; AAF05624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 88971 MW; 398AFC0980D99844 CRC64;
MPGGMGFPSD PALLPRVQAH IRKFPGTKYF KPELVAYDLQ QEHPEYQRKN HKVFMGMVRE
ALERIQLVAK EENDEKMEEK EAMDDVQEIP IVKALETRKR KAPAAGRKST GQAAAAKEVV
LSDDSEDERA ARQLEKQIES LKTNRANKTV LNLYTKKSAP STPVSTPKNQ ATKKPPGASA
APPALPRGLG AVSDTISPRE SHVKFEHIGG ADRQFLEVCR LAMHLKRPKT FATLGVDPPR
GFIVHGPPGC GKTMFAQAVA GELAIPMLQL AATELVSGVS GETEEKIRRL FDTAKQNSPC
ILILDDIDAI APRRETAQRE MERRVVSQLC SSLDELVLPP REKPLKDQLT FGDDGSVAII
GDSPTAAGAG VLVIGTTSRP DAVDGGLRRA GRFENEISLG IPDETAREKI LEKICKVNLA
GDVTLKQIAK LTPGYVGADL QALIREAAKV AIDRVFDTIV VKNEGHKNLT VEQIKEELDR
VLAWLQGDDD PSALSELNGG LQISFEDFER ALSTIQPAAK REGFATVPDV SWDDIGALVE
VRKQLEWSIL YPIKRADDFA ALGIDCRPQG ILLCGPPGCG KTLLAKAVAN ETGMNFISVK
GPELLNMYVG ESERAVRTVF QRARDSQPCV IFFDEIDALV PKRSHGESSG GARLVNQLLT
EMDGVEGRQK VFLIGATNRP DIVDAAILRP GRLDKILFVD FPSVEDRVDI LRKSTKNGTR
PMLGEDIDFH EIAQLPELAG FTGADLAALI HESSLLALQA RVLENDESVK GVGMRHFREA
ASRIRPSVTE ADRKKYEHMK KIYGLKQATP PSV
