ID   SEC5B_ARATH             Reviewed;        1090 AA.
AC   F4HWE6; Q9LMN3; Q9LPV1;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Exocyst complex component SEC5B;
DE            Short=AtSec5b;
GN   Name=SEC5B; OrderedLocusNames=At1g21170; ORFNames=F16F4.13, T22I11.1;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [4]
RP   COMPONENT OF THE EXOCYST COMPLEX, AND DISRUPTION PHENOTYPE.
RX   PubMed=18492870; DOI=10.1105/tpc.108.059105;
RA   Hala M., Cole R., Synek L., Drdova E., Pecenkova T., Nordheim A.,
RA   Lamkemeyer T., Madlung J., Hochholdinger F., Fowler J.E., Zarsky V.;
RT   "An exocyst complex functions in plant cell growth in Arabidopsis and
RT   tobacco.";
RL   Plant Cell 20:1330-1345(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19895414; DOI=10.1111/j.1469-8137.2009.03070.x;
RA   Chong Y.T., Gidda S.K., Sanford C., Parkinson J., Mullen R.T., Goring D.R.;
RT   "Characterization of the Arabidopsis thaliana exocyst complex gene families
RT   by phylogenetic, expression profiling, and subcellular localization
RT   studies.";
RL   New Phytol. 185:401-419(2010).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane during
CC       regulated or polarized secretion. Involved in polarized cell growth and
CC       organ morphogenesis. During cytokinesis, involved in cell plate
CC       initiation, cell plate maturation and formation of new primary cell
CC       wall.
CC   -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC       SEC10, EXO70A1 and EXO84B.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but the double mutant sec5a-1 and sec5b-1 is male
CC       gametophytic lethal due to defect in pollen germination and pollen tube
CC       growth. {ECO:0000269|PubMed:18492870}.
CC   -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF80645.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF81364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC012190; AAF80645.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC036104; AAF81364.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30072.1; -; Genomic_DNA.
DR   PIR; A86345; A86345.
DR   PIR; H86344; H86344.
DR   RefSeq; NP_173541.1; NM_101971.3.
DR   AlphaFoldDB; F4HWE6; -.
DR   SMR; F4HWE6; -.
DR   BioGRID; 23952; 1.
DR   STRING; 3702.AT1G21170.1; -.
DR   iPTMnet; F4HWE6; -.
DR   PaxDb; F4HWE6; -.
DR   PRIDE; F4HWE6; -.
DR   ProteomicsDB; 232861; -.
DR   EnsemblPlants; AT1G21170.1; AT1G21170.1; AT1G21170.
DR   GeneID; 838713; -.
DR   Gramene; AT1G21170.1; AT1G21170.1; AT1G21170.
DR   KEGG; ath:AT1G21170; -.
DR   Araport; AT1G21170; -.
DR   TAIR; locus:2199552; AT1G21170.
DR   eggNOG; KOG2347; Eukaryota.
DR   HOGENOM; CLU_003742_0_0_1; -.
DR   InParanoid; F4HWE6; -.
DR   OMA; ERTRINM; -.
DR   PRO; PR:F4HWE6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HWE6; baseline and differential.
DR   Genevisible; F4HWE6; AT.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0060321; P:acceptance of pollen; IGI:TAIR.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR029175; EXOC2/Sec5.
DR   InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR   PANTHER; PTHR13043; PTHR13043; 1.
DR   Pfam; PF15469; Sec5; 1.
DR   SUPFAM; SSF74788; SSF74788; 1.
PE   1: Evidence at protein level;
KW   Exocytosis; Phosphoprotein; Reference proteome; Transport.
FT   CHAIN           1..1090
FT                   /note="Exocyst complex component SEC5B"
FT                   /id="PRO_0000424570"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1079
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
SQ   SEQUENCE   1090 AA;  122673 MW;  9BFA42ECDF180537 CRC64;
     MSSSDDLDED ELLQMALKEQ SQRDVTYQKP PSANSRKPVT NLVQQPRRQK RAAAPPSKGG
     AKASRKPSMD EDDESEVELL SISSGDEDEG NDRGRGGGGD GGGGRGRGGS GKERGRARKE
     DDRAWDGVEP DCWKRVNEAE LARKVRDMRE SRTAPSVTQN LDRKVSGADK KVVLTSLQSF
     PRGMECIDPL KLGIIDNKTL RLITESSESL SKAEKVDNAL REKLVYTSDH FDPKLFISRI
     HQETSAADLE SGALALKSDL KGRNLQRKQL VKDNFDCFVS CKTTIDDIES KLKRIEDDPD
     GSGTTHLFNC MKSVTSRANR AFEPLFERQA QAEKIRSVQG MLQRFRTLFN LPSIIRSSIS
     KGEYDLAVRE YKKAKSIALP SHVNLLKRVL EEVEKVMQEF KGTLYRSMED PKIDFTSLEN
     TVRLLLELEP ESDPVWHYLN VQNHRIHGML EKCTFDHEAR MEILRNQVHE RALSDAKWRQ
     IQQNGVQLSD DTSSMEDNQV QVDQPLEESA RREKDALRGR YIKILTAVIV YHLPTFWKTA
     LSVFTGKFAK SSQVNDTSAS KAEEKAEEAR YSSHSLEEIA GMIRNTISVY EAKVQSTFHD
     FDESYILHPY MSDTIKEVSK ACQAFEAKES APHSAVMALR KVKVEITKIY IQRLCSWMRA
     STEEISKEET WIPVSILERN RSPYSISYLP LAFRSIIVSG MEQINMMILS LKGEAARSED
     MFAHIEEILI SVRLAFLNCF LDFAAHLEQI GADLSQRTTK RESWQNGYSN DHQEEQSINA
     PESVVDPHRQ LLMILSNIGY CKDELASELY NKYKYTWLQS RRNDEDISDL QDLMMSFSGL
     GEKVLEHYTF AKANLIRTAA TNYLLDSGIQ WGAAPPVKGI RDAAVELLHT LVAVHAEVFA
     GAKPLLDKIL GTLVEGLIDT FLSLLDENRS DDLSSIDANG FCQLMLELEY FETILKPYLT
     VDATESLKSL QGAVLEKAIE SISETVENNP GGHQRKPTRG SEDAISDDKQ SSVSPDDLLA
     LAQQCTSGML QLELEKTRLN SACFIETIPL DPVPPVAKAA YSRTSTDSPS RNYRESQPMG
     SPVQARPRRR