SIPL4_ARATH
ID SIPL4_ARATH Reviewed; 540 AA.
AC Q0WMJ8; Q9LQ94;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Signal peptide peptidase-like 4;
DE Short=AtSPPL4;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL4; OrderedLocusNames=At1g01650; ORFNames=T1N6.3;
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
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:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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=Q0WMJ8-1; Sequence=Displayed;
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=AAF78405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009273; AAF78405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27317.1; -; Genomic_DNA.
DR EMBL; AK229822; BAF01653.1; -; mRNA.
DR PIR; D86147; D86147.
DR RefSeq; NP_171671.2; NM_100047.4. [Q0WMJ8-1]
DR AlphaFoldDB; Q0WMJ8; -.
DR SMR; Q0WMJ8; -.
DR BioGRID; 24734; 1.
DR STRING; 3702.AT1G01650.1; -.
DR MEROPS; A22.A03; -.
DR MEROPS; A22.A05; -.
DR PaxDb; Q0WMJ8; -.
DR PRIDE; Q0WMJ8; -.
DR ProteomicsDB; 234548; -. [Q0WMJ8-1]
DR EnsemblPlants; AT1G01650.1; AT1G01650.1; AT1G01650. [Q0WMJ8-1]
DR GeneID; 839499; -.
DR Gramene; AT1G01650.1; AT1G01650.1; AT1G01650. [Q0WMJ8-1]
DR KEGG; ath:AT1G01650; -.
DR Araport; AT1G01650; -.
DR TAIR; locus:2198155; AT1G01650.
DR eggNOG; KOG2442; Eukaryota.
DR InParanoid; Q0WMJ8; -.
DR PhylomeDB; Q0WMJ8; -.
DR PRO; PR:Q0WMJ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WMJ8; baseline and differential.
DR Genevisible; Q0WMJ8; AT.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..540
FT /note="Signal peptide peptidase-like 4"
FT /id="PRO_0000419096"
FT TOPO_DOM 27..195
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..431
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..170
FT /note="PA"
FT MOTIF 494..496
FT /note="PAL"
FT ACT_SITE 387
FT /evidence="ECO:0000250"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 540 AA; 59971 MW; F00F15130903F6CA CRC64;
MILWKSLSCF SFVFGLLLYS ASFVCAGDIV HHDDSLPQRP GCNNNFVLVK VPTRVNGSEY
TEYVGVGARF GPTLESKEKH ATLIKLAIAD PPDCCSTPKN KLTGEVILVH RGKCSFTTKT
KVAEAAGASA ILIINNSTDL FKMVCEKGEN VLDITIPVVM LPVDAGRSLE NIVKSNAIVT
LQLYSPKRPA VDVAEVFLWL MAVGTILCAS YWSAWTVREE AIEQDKLLKD GSDELLQLST
TSSRGVVEVT VISAILFVVV ASCFLIMLYK LMSFWFIEVL VVLFCIGGVE GLQTCLVSLL
SCFRWFRRFG ESYVKVPFLG AVSYLTLAIC PFCIAFAVFW AVKRQYSYAW IGQDILGISL
IITVLQIVRV PNLKVGFVLL SCAFMYDIFW VFVSKWWFRE SVMIVVARGD RSGEDGIPML
LKIPRMFDPW GGYSIIGFGD IILPGLLVTF ALRYDWLANK RLKSGYFLGT MSAYGLGLLI
TYIALNLMDG HGQPALLYIV PFILGTLFVL GHKRGDLKTL WTTGEPDRPC PHVRLQPQSS
