ID   MEM11_ARATH             Reviewed;         225 AA.
AC   Q9SJL6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Membrin-11;
DE            Short=AtMEMB11;
DE   AltName: Full=27 kDa Golgi SNARE protein;
DE   AltName: Full=Golgi SNAP receptor complex member 2-1;
GN   Name=MEMB11; OrderedLocusNames=At2g36900; ORFNames=T1J8.8;
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   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).
CC   -!- FUNCTION: Involved in transport of proteins from the cis/medial-Golgi
CC       to the trans-Golgi network. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type IV membrane protein {ECO:0000305}.
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=Q9SJL6-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the GOSR2 family. {ECO:0000305}.
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DR   EMBL; AC006922; AAD31575.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09318.1; -; Genomic_DNA.
DR   EMBL; AY063816; AAL36172.1; -; mRNA.
DR   EMBL; AY091350; AAM14289.1; -; mRNA.
DR   EMBL; AY086341; AAM64409.1; -; mRNA.
DR   PIR; A84786; A84786.
DR   RefSeq; NP_181227.1; NM_129246.3. [Q9SJL6-1]
DR   AlphaFoldDB; Q9SJL6; -.
DR   SMR; Q9SJL6; -.
DR   BioGRID; 3608; 2.
DR   IntAct; Q9SJL6; 2.
DR   STRING; 3702.Q9SJL6; -.
DR   iPTMnet; Q9SJL6; -.
DR   PaxDb; 3702-AT2G36900-1; -.
DR   ProteomicsDB; 250682; -. [Q9SJL6-1]
DR   EnsemblPlants; AT2G36900.1; AT2G36900.1; AT2G36900. [Q9SJL6-1]
DR   GeneID; 818264; -.
DR   Gramene; AT2G36900.1; AT2G36900.1; AT2G36900. [Q9SJL6-1]
DR   KEGG; ath:AT2G36900; -.
DR   Araport; AT2G36900; -.
DR   TAIR; AT2G36900; MEMB11.
DR   eggNOG; KOG3251; Eukaryota.
DR   HOGENOM; CLU_083740_1_0_1; -.
DR   InParanoid; Q9SJL6; -.
DR   OMA; RMRVDQL; -.
DR   PhylomeDB; Q9SJL6; -.
DR   PRO; PR:Q9SJL6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJL6; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd15863; SNARE_GS27; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR027027; GOSR2/Membrin/Bos1.
DR   PANTHER; PTHR21230:SF1; GOLGI SNAP RECEPTOR COMPLEX MEMBER 2; 1.
DR   PANTHER; PTHR21230; VESICLE TRANSPORT V-SNARE PROTEIN VTI1-RELATED; 1.
DR   Pfam; PF12352; V-SNARE_C; 1.
DR   PIRSF; PIRSF028865; Membrin-2; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   Genevisible; Q9SJL6; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Golgi apparatus; Membrane;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..225
FT                   /note="Membrin-11"
FT                   /id="PRO_0000212554"
FT   TOPO_DOM        2..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..225
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   225 AA;  25628 MW;  BF92037DD3D63A22 CRC64;
     MASGIVEGGG SLSDVYSSAK RILLKARDGI ERLERFESSS MDSPDLASSV KRDITEVRSL
     CSNMDTLWRS IPVKSQRDLW RRKTEQVGEE AEYLNLSLEK YMSRNQRKML EAKERADLLG
     RASGEGAHIL QIFDEEAQAM SSVKNSKRML EESFSSGVAI LSKYAEQRDR LKSAQRKALD
     VLNTVGLSNS VLRLIERRNR VDTWIKYAGM IATLVILYLF IRWTR
//