ID A0A0D2S5Z2_GOSRA Unreviewed; 904 AA.
AC A0A0D2S5Z2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=B456_007G030900 {ECO:0000313|EMBL:KJB39794.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB39794.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB39794.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM001746; KJB39794.1; -; Genomic_DNA.
DR RefSeq; XP_012488826.1; XM_012633372.1.
DR RefSeq; XP_012488827.1; XM_012633373.1.
DR AlphaFoldDB; A0A0D2S5Z2; -.
DR STRING; 29730.A0A0D2S5Z2; -.
DR EnsemblPlants; KJB39794; KJB39794; B456_007G030900.
DR Gramene; KJB39794; KJB39794; B456_007G030900.
DR eggNOG; KOG2004; Eukaryota.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000032304; Chromosome 7.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 11..268
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 707..892
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 67..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 902..904
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT COMPBIAS 67..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 798
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 841
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 423..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 904 AA; 100302 MW; C63ED88331E7E42B CRC64;
MAESVELPGR LAILPFRNKV LLPGAFIRIR CTSQSSVKLV EQELWQREEK GLIGILPVQD
AAETTSMDSM LSQGVGSESG ERSSNVQVST SDAHKVDGKN PSEVIHWHNR GVAARALHLS
RGVEKPSGRV TYIVVLEGLC RFNIEELNTR GPYCTAKISP LEMTKSGYFL ISIFYLLTCL
EMEQVEQDPD FVTLSRQFKA IAMELISILE QKQKTGGRIK VLLETLPFHK LADIFVASFE
ISFEEQLCML DSVDPKVRLS KATELVDRHL QSIRVAEKIT QKVEGQLSKS QKEYLLRQQM
RAIKEELGDN DDDEDDLASL ERKMQNAGMP SNIWKHAQRE LRRLKKMQPQ QPGYNSSRVY
LDLLADLPWQ KASEEQELDL KAAKDHLDCD HYGLVKIKQR IIEYLAVRKL KPDARGPVLC
FVGPPGVGKT SLASSIAAAL GRKFIRISLG GVKDEADIRG HRRTYIGSMP GRLIDGLKRV
GVCNPVMLLD EIDKTGSDVR GDPASALLEV LDPEQNKSFN DHYLNVPFDL SKVIFVATAN
RMQPIPPPLL DRMEVIELPG YTAEEKLRIA MQHLIPRVLD QHGLSSAFLQ IPEDMVKLVI
QRYTREAGVR NLERNLAALA RAAAVRVAER EQAVSVSKDV HKITSPLLDN RLAEGAEMEM
EVIPMVVNNH EISNAFRIAS PLVVDEAMLE KILGPPRFDD QEAADRVATP GVSVGLVWTA
FGGEVQFVEA TSVVGNGELR LTGQLGDVIK ESAQIALTWV RARVEDLKLA AAEETDLLQG
KDIHIHFPAG AVPKDGPSAG VTLVTALVSL FSQKNVRADT AMTGEMTLRG LVLPVGGVKD
KVLAAHRYGI KRVILPERNL KDLVEVPADV LSSLEILVAK RMEDVLEHAF DGGCPWRQHQ
HSKL
//
