ID   STLP2_ARATH             Reviewed;         393 AA.
AC   Q39221; Q7EP29; Q8VZ72;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 4.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=SEC12-like protein 2;
GN   Name=STL2P; Synonyms=ST12P; OrderedLocusNames=At2g01470; ORFNames=F2I9.9;
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 [MRNA], AND FUNCTION.
RX   PubMed=1396601; DOI=10.1002/j.1460-2075.1992.tb05514.x;
RA   d'Enfert C., Gensse M., Gaillardin C.;
RT   "Fission yeast and a plant have functional homologues of the Sar1 and Sec12
RT   proteins involved in ER to Golgi traffic in budding yeast.";
RL   EMBO J. 11:4205-4211(1992).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [7]
RP   INTERACTION WITH BZIP28.
RX   PubMed=22335396; DOI=10.1111/j.1365-313x.2012.04943.x;
RA   Srivastava R., Chen Y., Deng Y., Brandizzi F., Howell S.H.;
RT   "Elements proximal to and within the transmembrane domain mediate the
RT   organelle-to-organelle movement of bZIP28 under ER stress conditions.";
RL   Plant J. 70:1033-1042(2012).
CC   -!- FUNCTION: Required for the formation or budding of transport vesicles
CC       from the ER. {ECO:0000269|PubMed:1396601}.
CC   -!- SUBUNIT: Interacts with BZIP28. {ECO:0000269|PubMed:22335396}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi
CC       network membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000250}. Note=Endoplasmic reticulum and the early Golgi.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: In the process of transport, may migrate to the Golgi
CC       apparatus and function in subsequent transport events. {ECO:0000250}.
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DR   EMBL; M95796; AAA32871.1; -; mRNA.
DR   EMBL; AC005560; AAC67323.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05458.1; -; Genomic_DNA.
DR   EMBL; AY065198; AAL38374.1; -; mRNA.
DR   EMBL; AY074332; AAL67028.1; -; mRNA.
DR   EMBL; AY123030; AAM67563.1; -; mRNA.
DR   PIR; B84425; B84425.
DR   PIR; S28604; S28604.
DR   PIR; T48907; T48907.
DR   RefSeq; NP_178256.1; NM_126208.4.
DR   AlphaFoldDB; Q39221; -.
DR   SMR; Q39221; -.
DR   BioGRID; 78; 4.
DR   STRING; 3702.AT2G01470.1; -.
DR   iPTMnet; Q39221; -.
DR   MetOSite; Q39221; -.
DR   PaxDb; Q39221; -.
DR   PRIDE; Q39221; -.
DR   ProteomicsDB; 245217; -.
DR   EnsemblPlants; AT2G01470.1; AT2G01470.1; AT2G01470.
DR   GeneID; 814675; -.
DR   Gramene; AT2G01470.1; AT2G01470.1; AT2G01470.
DR   KEGG; ath:AT2G01470; -.
DR   Araport; AT2G01470; -.
DR   TAIR; locus:2049582; AT2G01470.
DR   eggNOG; KOG0771; Eukaryota.
DR   HOGENOM; CLU_058136_0_0_1; -.
DR   InParanoid; Q39221; -.
DR   OMA; KAHEFPP; -.
DR   OrthoDB; 828247at2759; -.
DR   PhylomeDB; Q39221; -.
DR   PRO; PR:Q39221; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q39221; baseline and differential.
DR   Genevisible; Q39221; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:TAIR.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR045260; Sec12-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   PANTHER; PTHR23284; PTHR23284; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..393
FT                   /note="SEC12-like protein 2"
FT                   /id="PRO_0000051229"
FT   TOPO_DOM        2..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          151..190
FT                   /note="WD 1"
FT   REPEAT          193..231
FT                   /note="WD 2"
FT   REPEAT          283..322
FT                   /note="WD 3"
FT   REPEAT          326..367
FT                   /note="WD 4"
FT   REGION          40..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   CONFLICT        322
FT                   /note="V -> I (in Ref. 1; AAA32871)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  42794 MW;  D076454309A15013 CRC64;
     MANQSTETNQ PSNMQTYGVP IYAADWIPEV DVRSKIIMDP EKSEDDDESS SSSSSSRSCI
     VLSGGGGEGR SGISNVILIC RVDLNTNSLS EQPLGRLVVG SDLPYRMAVH PREGGLICAL
     PNSCKLFHWE DIMSREDNQA GESEEVIKEL RDVGQQLALA FNPEGSVLAA GAEDGTLRVF
     KWPSMNTLLN ESQAHSSVKC LTFSESGQFL VSLGGPVCRV WDVNASAAVA SLSKEKDEMF
     ASCRFSVDSA GNEVLYIAAN TERGGSIITC DTKLWKRKWS KPIKKNSISA FNVSADGKLL
     AIGTLEGDVL ILESTRMQTI QVVKKAHLGL VTALTFSPDS RGLVSVSFDS RARLTMIEQK
     GDKPGVRWWL LVLLIVLLYV VAYYYMKAKG IIP