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SIPL4_ORYSJ
ID   SIPL4_ORYSJ             Reviewed;         545 AA.
AC   Q0DWA9; A0A0P0VRF0; Q6K9X7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Signal peptide peptidase-like 4;
DE            Short=OsSPPL4;
DE            EC=3.4.23.-;
DE   Flags: Precursor;
GN   Name=SPPL4; OrderedLocusNames=Os02g0823000, LOC_Os02g57710;
GN   ORFNames=OJ1136_C04.4, OsJ_08929;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19688213; DOI=10.1007/s00299-009-0760-9;
RA   Tamura T., Kuroda M., Oikawa T., Kyozuka J., Terauchi K., Ishimaru Y.,
RA   Abe K., Asakura T.;
RT   "Signal peptide peptidases are expressed in the shoot apex of rice,
RT   localized to the endoplasmic reticulum.";
RL   Plant Cell Rep. 28:1615-1621(2009).
CC   -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC       cleaves type II membrane signal peptides in the hydrophobic plane of
CC       the membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC       {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD22919.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EEE58070.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP004026; BAD22919.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008208; BAF10479.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS81654.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE58070.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK122065; BAH00778.1; -; mRNA.
DR   RefSeq; XP_015625571.1; XM_015770085.1.
DR   AlphaFoldDB; Q0DWA9; -.
DR   SMR; Q0DWA9; -.
DR   STRING; 4530.OS02T0823000-01; -.
DR   MEROPS; A22.A05; -.
DR   PaxDb; Q0DWA9; -.
DR   PRIDE; Q0DWA9; -.
DR   EnsemblPlants; Os02t0823000-01; Os02t0823000-01; Os02g0823000.
DR   GeneID; 4331193; -.
DR   Gramene; Os02t0823000-01; Os02t0823000-01; Os02g0823000.
DR   KEGG; osa:4331193; -.
DR   eggNOG; KOG2442; Eukaryota.
DR   HOGENOM; CLU_023799_4_1_1; -.
DR   InParanoid; Q0DWA9; -.
DR   OMA; LSKDYCM; -.
DR   OrthoDB; 535101at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q0DWA9; OS.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; IBA:GO_Central.
DR   GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR   GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IBA:GO_Central.
DR   GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007369; Peptidase_A22B_SPP.
DR   InterPro; IPR006639; Preselin/SPP.
DR   PANTHER; PTHR12174; PTHR12174; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04258; Peptidase_A22B; 1.
DR   SMART; SM00730; PSN; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..545
FT                   /note="Signal peptide peptidase-like 4"
FT                   /id="PRO_0000419103"
FT   TOPO_DOM        26..193
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..276
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..317
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..343
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..427
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..485
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        507..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          90..170
FT                   /note="PA"
FT   MOTIF           490..492
FT                   /note="PAL"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        436
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  59885 MW;  E7AA697598933CEC CRC64;
     MGTSSPEMAA ALLLVMAALA GVAAGGDIVH QDDEAPKIPG CSNDFVLVKV QTWVNNREDG
     EFVGVGARFG PTIESKEKHA NRTGLLLADP IDCCDPPTQK VAGDVLLVQR GNCKFTKKAK
     NAEAAGASAI IIINHVHELY KMVCDRNETD LDINIPAVLL PKDAGNDLQK LLTRGKVSVQ
     LYSPDRPLVD TAEVFLWLMA VGTILCASYW SAWSAREAVI EQEKLLKDGH ESSLNLEAGG
     SSGMVDINMT SAILFVVIAS CFLIMLYKLM SHWFVELLVV IFCIGGVEGL QTCLVALLSR
     WFKPAAESFV KVPFFGAVSY LTIAVCPFCI VFAVIWAVYR RMTYAWIGQD ILGIALIVTV
     IQIVRIPNLK VGSVLLSCSF LYDIFWVFIS KMWFHESVMI VVARGDKTDE DGVPMLLKIP
     RMFDPWGGFS IIGFGDILLP GLLIAFALRY DWAAKKTLQS GYFLWSMVAY GSGLMITYVA
     LNLMDGHGQP ALLYIVPFTL GTFIALGRKR GELRNLWTRG QPERVCTHMH MQPSPKDTNC
     DAVSS
 
 
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