SIP_ARATH
ID SIP_ARATH Reviewed; 344 AA.
AC O81062; Q8LAP9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Signal peptide peptidase;
DE Short=AtSPP;
DE EC=3.4.23.-;
DE AltName: Full=Intramembrane protease;
DE Short=IMP;
DE Short=IMPAS;
GN Name=SPP; OrderedLocusNames=At2g03120; ORFNames=T18E12.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18067581; DOI=10.1111/j.1742-4658.2007.06170.x;
RA Tamura T., Asakura T., Uemura T., Ueda T., Terauchi K., Misaka T., Abe K.;
RT "Signal peptide peptidase and its homologs in Arabidopsis thaliana - plant
RT tissue-specific expression and distinct subcellular localization.";
RL FEBS J. 275:34-43(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19168645; DOI=10.1104/pp.108.130252;
RA Han S., Green L., Schnell D.J.;
RT "The signal peptide peptidase is required for pollen function in
RT Arabidopsis.";
RL Plant Physiol. 149:1289-1301(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 (By similarity). Catalyzes intramembrane proteolysis of
CC some signal peptides after they have been cleaved from a preprotein,
CC resulting in the release of the fragment from the ER membrane into the
CC cytoplasm (By similarity). Plays a critical role in the development and
CC function of the reproductive tissues, especially in pollen development.
CC {ECO:0000250, ECO:0000269|PubMed:19168645}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18067581, ECO:0000269|PubMed:19168645}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18067581,
CC ECO:0000269|PubMed:19168645}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with the highest expression in emerging
CC leaves, roots, and floral tissues (at the protein level). Highly
CC detected in pollen. {ECO:0000269|PubMed:18067581,
CC ECO:0000269|PubMed:19168645}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the shoot meristem and root epidermal
CC cells in germinating seeds. At the reproductive stage, expressed in the
CC whole shoot apex. {ECO:0000269|PubMed:18067581}.
CC -!- DOMAIN: The first transmembrane domain may act as a type I signal
CC anchor. The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mostly lethal due to a male gametophytic defect.
CC {ECO:0000269|PubMed:19168645}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
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DR EMBL; AC005313; AAC34490.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05665.1; -; Genomic_DNA.
DR EMBL; AY065169; AAL38345.1; -; mRNA.
DR EMBL; AY114571; AAM47890.1; -; mRNA.
DR EMBL; AY087685; AAM65222.1; -; mRNA.
DR PIR; T02714; T02714.
DR RefSeq; NP_565294.1; NM_126363.7.
DR AlphaFoldDB; O81062; -.
DR BioGRID; 243; 9.
DR IntAct; O81062; 8.
DR STRING; 3702.AT2G03120.1; -.
DR MEROPS; A22.A15; -.
DR PaxDb; O81062; -.
DR PRIDE; O81062; -.
DR ProteomicsDB; 234465; -.
DR EnsemblPlants; AT2G03120.1; AT2G03120.1; AT2G03120.
DR GeneID; 814841; -.
DR Gramene; AT2G03120.1; AT2G03120.1; AT2G03120.
DR KEGG; ath:AT2G03120; -.
DR Araport; AT2G03120; -.
DR TAIR; locus:2056936; AT2G03120.
DR eggNOG; KOG2443; Eukaryota.
DR HOGENOM; CLU_023799_0_1_1; -.
DR InParanoid; O81062; -.
DR OMA; LFSYEDH; -.
DR OrthoDB; 1087991at2759; -.
DR PhylomeDB; O81062; -.
DR BRENDA; 3.4.23.B24; 399.
DR PRO; PR:O81062; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81062; baseline and differential.
DR Genevisible; O81062; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
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:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IBA:GO_Central.
DR GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR033154; AtSSP.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR PANTHER; PTHR12174:SF88; PTHR12174:SF88; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Signal peptide peptidase"
FT /id="PRO_0000419092"
FT TOPO_DOM 1..11
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..230
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..290
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..292
FT /note="PAL"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /evidence="ECO:0000250"
FT CONFLICT 294
FT /note="Y -> F (in Ref. 4; AAM65222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38339 MW; 4065996ED065FFCF CRC64;
MKNCERFANL ALAGLTLAPL VVRVNPNLNV ILTACITVYV GCFRSVKDTP PTETMSKEHA
MRFPLVGSAM LLSLFLLFKF LSKDLVNAVL TAYFFVLGIV ALSATLLPAI RRFLPNPWND
NLIVWRFPYF KSLEVEFTKS QVVAGIPGTF FCAWYAWKKH WLANNILGLS FCIQGIEMLS
LGSFKTGAIL LAGLFFYDIF WVFFTPVMVS VAKSFDAPIK LLFPTGDALR PYSMLGLGDI
VIPGIFVALA LRFDVSRRRQ PQYFTSAFIG YAVGVILTIV VMNWFQAAQP ALLYIVPAVI
GFLASHCIWN GDIKPLLAFD ESKTEEATTD ESKTSEEVNK AHDE
