GenomeNet

Database: UniProt
Entry: A0A1U8IG25_GOSHI
LinkDB: A0A1U8IG25_GOSHI
Original site: A0A1U8IG25_GOSHI 
ID   A0A1U8IG25_GOSHI        Unreviewed;       256 AA.
AC   A0A1U8IG25;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE            EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
GN   Name=LOC107894556 {ECO:0000313|RefSeq:XP_016675308.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016675308.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016675308.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016675308.1};
RG   RefSeq;
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|RuleBase:RU366005};
CC       Note=Binds 1 zinc ion per subunit. {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   RefSeq; XP_016675308.1; XM_016819819.1.
DR   AlphaFoldDB; A0A1U8IG25; -.
DR   STRING; 3635.A0A1U8IG25; -.
DR   PaxDb; 3635-A0A1U8IG25; -.
DR   GeneID; 107894556; -.
DR   KEGG; ghi:107894556; -.
DR   OrthoDB; 3080668at2759; -.
DR   Proteomes; UP000189702; Chromosome 15.
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; IBA:GO_Central.
DR   GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
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|RuleBase:RU366005};
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:UP000189702};
KW   Transmembrane {ECO:0000256|RuleBase:RU366005};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU366005};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366005}.
FT   TRANSMEM        56..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366005"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366005"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366005"
FT   DOMAIN          22..196
FT                   /note="CAAX prenyl protease 1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16491"
FT   DOMAIN          200..256
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   256 AA;  29423 MW;  6DCB5105D77A795A CRC64;
     MEVPGFLILM YLFETYLDLR QHATLKLPTL PKTLEAVISQ EKFEKSRAYS LDKSHFYFVH
     EFVTILIDSA ILFFGILPWF WKKSGTFLPL LGLIEENEIL HTLSFLAGAM IWSQITDLPF
     SLYSTFVIEA RHGFNKQTIW LFFRDLIKGI CLAIVLGPPI VSAIIVIVQS GGPYLAIYLW
     AFMFVLSLVI APLFNKFTPL PEGELKLKIE KLAFSLKFSL KKLFVVNGST RSSYSNAYMY
     CFFKNKPIVL YDTLIQ
//
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