SIPL2_ARATH
ID SIPL2_ARATH Reviewed; 540 AA.
AC Q8W469; Q8LCK4; Q9CAD4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Signal peptide peptidase-like 2;
DE Short=AtSPPL2;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL2; OrderedLocusNames=At1g63690; ORFNames=F24D7.12;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
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:0000269|PubMed:18067581};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18067581}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W469-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18067581}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the shoot meristem and root epidermal
CC cells in germinating seeds. {ECO:0000269|PubMed:18067581}.
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=AAG52428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011622; AAG52428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34134.1; -; Genomic_DNA.
DR EMBL; AY062807; AAL32885.1; -; mRNA.
DR EMBL; BT008895; AAP68334.1; -; mRNA.
DR EMBL; AY086545; AAM63609.1; -; mRNA.
DR PIR; H96661; H96661.
DR RefSeq; NP_564815.1; NM_105046.3. [Q8W469-1]
DR AlphaFoldDB; Q8W469; -.
DR SMR; Q8W469; -.
DR BioGRID; 27894; 1.
DR STRING; 3702.AT1G63690.1; -.
DR MEROPS; A22.A05; -.
DR PaxDb; Q8W469; -.
DR PRIDE; Q8W469; -.
DR ProteomicsDB; 232536; -. [Q8W469-1]
DR EnsemblPlants; AT1G63690.1; AT1G63690.1; AT1G63690. [Q8W469-1]
DR GeneID; 842673; -.
DR Gramene; AT1G63690.1; AT1G63690.1; AT1G63690. [Q8W469-1]
DR KEGG; ath:AT1G63690; -.
DR Araport; AT1G63690; -.
DR eggNOG; KOG2442; Eukaryota.
DR HOGENOM; CLU_023799_4_1_1; -.
DR InParanoid; Q8W469; -.
DR PhylomeDB; Q8W469; -.
DR PRO; PR:Q8W469; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W469; baseline and differential.
DR Genevisible; Q8W469; AT.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
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 Alternative splicing; Endosome; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..540
FT /note="Signal peptide peptidase-like 2"
FT /id="PRO_0000419094"
FT TOPO_DOM 28..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..278
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..345
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..429
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..488
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 95..173
FT /note="PA"
FT MOTIF 492..494
FT /note="PAL"
FT ACT_SITE 385
FT /evidence="ECO:0000250"
FT ACT_SITE 438
FT /evidence="ECO:0000250"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 13
FT /note="S -> L (in Ref. 4; AAM63609)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="W -> C (in Ref. 4; AAM63609)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> T (in Ref. 4; AAM63609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 59837 MW; 4E7EF475C1C06293 CRC64;
MDSLRFLRIL LLSSSILLLS LRSTVTAGDI VHQDNLAPKK PGCENDFVLV KVQTWIDGVE
NEEFVGVGAR FGKRIVSKEK NANQTHLVFA NPRDSCTPLK NKLSGDVVIV ERGNCRFTAK
ANNAEAAGAS ALLIINNQKE LYKMVCEPDE TDLDIQIPAV MLPQDAGASL QKMLANSSKV
SAQLYSPRRP AVDVAEVFLW LMAIGTILCA SYWSAWSARE AAIEHDKLLK DAIDEIPNTN
DGGSGVVEIN SISAIFFVVL ASGFLVILYK LMSYWFVELL VVVFCIGGVE GLQTCLVALL
SRWFQRAADT YVKVPFLGPI SYLTLAVSPF CIVFAVLWAV YRVHSFAWIG QDVLGIALII
TVLQIVHVPN LKVGTVLLSC AFLYDIFWVF VSKKLFHESV MIVVARGDKS GEDGIPMLLK
IPRMFDPWGG YSIIGFGDIL LPGLLIAFAL RYDWLANKTL RTGYFIWAMV AYGLGLLITY
VALNLMDGHG QPALLYIVPF TLGTMLTLAR KRDDLWILWT KGEPERACPH HVRLEQCSEK
