ID A0A3Q3WFB5_MOLML Unreviewed; 443 AA.
AC A0A3Q3WFB5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000013368.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000013368.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family.
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU366005}.
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DR AlphaFoldDB; A0A3Q3WFB5; -.
DR STRING; 94237.ENSMMOP00000013368; -.
DR Ensembl; ENSMMOT00000013589.1; ENSMMOP00000013368.1; ENSMMOG00000010265.1.
DR OMA; FVIEEKF; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:UniProtKB-UniRule.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU366005};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366005};
KW Membrane {ECO:0000256|RuleBase:RU366005};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366005};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366005};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Transmembrane {ECO:0000256|RuleBase:RU366005};
KW Transmembrane helix {ECO:0000256|RuleBase:RU366005};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT DOMAIN 36..220
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 224..438
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 286..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 387
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 443 AA; 50513 MW; 7BD743A191F8616F CRC64;
MVESIFDLPV EKQIFYAVLG FSWTVYVWEA YLSYRQRRIY RSTTHVPQEL GKIMDSETFE
KSRLYQLDKS NFSFWSGLYS ETEGTLILLL GGIPFLWGVA GSVTARFGFG SEYEITQSLI
FLMLATLFSA LTGLPWSLYN TFVIEEKHGF NQQTIGFFLK DAVKKFVVTQ CILLPVTSLL
LYIIKIGGDY FFIYAWLFTL AVSLVLVTIY ADYIAPLFDK FTPLPEGELK TDIEAMAKSI
SFPLTKVYVV EGSKRSSHSN AYFYGFFKNK RIVLFDTLLE DYSPLNKGES QPEQPESNEA
SGESKAKPKN KKQGCNNPEI LAVLGHELGH WKLGHTVKNI VISQVINYEF FPVLLPVCCS
DRTLDDYLPL LSFCLTVLSR RFEFQADAFA RGMGKASELY SALIKLNKDN LGFPVADWLF
SMWHYSHPPL LERLRALGNV KQD
//
