SAB_ARATH
ID SAB_ARATH Reviewed; 2603 AA.
AC Q6IMT1; F4I9T5; Q0WN66; Q38969; Q9C6Q6; Q9C727;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Protein SABRE {ECO:0000303|PubMed:8275864};
DE AltName: Full=Protein HYPERSENSITIVE TO PI STARVATION 4 {ECO:0000303|PubMed:22615140};
DE Flags: Precursor;
GN Name=SAB {ECO:0000303|PubMed:8275864};
GN Synonyms=HPS4 {ECO:0000303|PubMed:22615140};
GN OrderedLocusNames=At1g58250 {ECO:0000312|Araport:AT1G58250};
GN ORFNames=F16M22.5 {ECO:0000312|EMBL:AAG50951.1},
GN T18I24.18 {ECO:0000312|EMBL:AAG50770.1};
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 {ECO:0000312|EMBL:DAA00365.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14675453; DOI=10.1046/j.1365-313x.2003.01933.x;
RA Procissi A., Guyon A., Pierson E.S., Giritch A., Knuiman B., Grandjean O.,
RA Tonelli C., Derksen J., Pelletier G., Bonhomme S.;
RT "KINKY POLLEN encodes a SABRE-like protein required for tip growth in
RT Arabidopsis and conserved among eukaryotes.";
RL Plant J. 36:894-904(2003).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 [GENOMIC DNA] OF 1257-2603, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=7867930; DOI=10.1101/gad.9.3.330;
RA Aeschbacher R.A., Hauser M.-T., Feldmann K.A., Benfey P.N.;
RT "The SABRE gene is required for normal cell expansion in Arabidopsis.";
RL Genes Dev. 9:330-340(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-2603.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8275864; DOI=10.1242/dev.119.supplement.57;
RA Benfey P.N., Linstead P.J., Roberts K., Schiefelbein J.W., Hauser M.-T.,
RA Aeschbacher R.A.;
RT "Root development in Arabidopsis: four mutants with dramatically altered
RT root morphogenesis.";
RL Development 119:57-70(1993).
RN [7]
RP FUNCTION, MUTAGENESIS OF ALA-2118, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22615140; DOI=10.1093/jxb/ers131;
RA Yu H., Luo N., Sun L., Liu D.;
RT "HPS4/SABRE regulates plant responses to phosphate starvation through
RT antagonistic interaction with ethylene signalling.";
RL J. Exp. Bot. 63:4527-4538(2012).
CC -!- FUNCTION: May be involved in membrane trafficking (By similarity).
CC Required for cell expansion, especially in root cortex, probably by
CC counteracting the action of ethylene in promoting cells radial
CC expansion (PubMed:7867930, PubMed:8275864). Involved in female organ
CC development (PubMed:14675453). Antagonistically interacts with ethylene
CC signaling to regulate plant responses to Pi starvation
CC (PubMed:22615140). {ECO:0000250|UniProtKB:K7VLR4,
CC ECO:0000269|PubMed:14675453, ECO:0000269|PubMed:22615140,
CC ECO:0000269|PubMed:7867930, ECO:0000269|PubMed:8275864}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6IMT0}. Golgi
CC apparatus {ECO:0000250|UniProtKB:K7VLR4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q6IMT1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highest levels in leaves, also expressed in leaves,
CC flowers, and siliques, and, to a lower extent, in roots and stems.
CC {ECO:0000269|PubMed:22615140}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, expressed in hypocotyl and in the
CC entire cotyledon. Observed in all types of cells in the root apex, but
CC restricted to vascular tissue in the upper part of the root. Stronger
CC expression in young leaves than in old leaves. Accumulates in all
CC flower organs, including the sepal, petal, stamen, and gynoecium. In
CC the silique, high levels at both ends but weak in the middle.
CC {ECO:0000269|PubMed:22615140}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants; smaller aerial organs and wider
CC roots because of abnormal diffuse cell growth. Abnormal cell expansion
CC that is greatest in the root cortex cell layer and is independent of
CC the root growth rate, and that leads to a shift in the orientation of
CC expansion (PubMed:7867930, PubMed:8275864). Sterility due to female
CC organ anomalies (PubMed:8275864, PubMed:14675453). Enhanced responses
CC to Pi starvation (PubMed:22615140). {ECO:0000269|PubMed:14675453,
CC ECO:0000269|PubMed:22615140, ECO:0000269|PubMed:7867930,
CC ECO:0000269|PubMed:8275864}.
CC -!- MISCELLANEOUS: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ third party annotation (TPA) entry.
CC -!- SIMILARITY: Belongs to the SABRE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE33523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF01434.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BK000517; DAA00365.1; -; mRNA.
DR EMBL; AC073943; AAG50951.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079131; AAG50770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AH006602; AAC49734.1; -; Genomic_DNA.
DR EMBL; AK229585; BAF01434.1; ALT_FRAME; mRNA.
DR PIR; A96616; A96616.
DR RefSeq; NP_176121.3; NM_104605.4.
DR AlphaFoldDB; Q6IMT1; -.
DR SMR; Q6IMT1; -.
DR STRING; 3702.AT1G58250.2; -.
DR PaxDb; Q6IMT1; -.
DR PRIDE; Q6IMT1; -.
DR ProteomicsDB; 226682; -. [Q6IMT1-1]
DR GeneID; 842193; -.
DR KEGG; ath:AT1G58250; -.
DR Araport; AT1G58250; -.
DR eggNOG; KOG1910; Eukaryota.
DR PRO; PR:Q6IMT1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6IMT1; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:UniProtKB.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR InterPro; IPR045167; FMP27.
DR InterPro; IPR019443; FMP27_C.
DR InterPro; IPR019441; FMP27_GFWDK_dom.
DR PANTHER; PTHR15678; PTHR15678; 1.
DR Pfam; PF10351; Apt1; 1.
DR Pfam; PF10347; Fmp27_GFWDK; 1.
DR SMART; SM01214; Fmp27_GFWDK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein; Glycoprotein;
KW Golgi apparatus; Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..2603
FT /note="Protein SABRE"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432482"
FT REGION 259..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1717..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2339..2380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2448..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2554..2603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1995..2023
FT /evidence="ECO:0000255"
FT COMPBIAS 259..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2343..2380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2448..2466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 2118
FT /note="A->P: In hps4; enhanced responses to Pi starvation,
FT including increased inhibition of primary root growth,
FT probably due to an increased auxin accumulation in root
FT tips, enhanced expression of Pi starvation-induced genes,
FT and overproduction of root-associated acid phosphatases
FT (APase)."
FT /evidence="ECO:0000269|PubMed:22615140"
FT CONFLICT 1898
FT /note="K -> N (in Ref. 4; AAC49734)"
FT /evidence="ECO:0000305"
FT CONFLICT 2239
FT /note="A -> S (in Ref. 4; AAC49734)"
FT /evidence="ECO:0000305"
FT CONFLICT 2464
FT /note="N -> D (in Ref. 5; BAF01434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2603 AA; 292913 MW; 509E210A22858ACF CRC64;
MAASPAKFFF GFLIVSIVLW MIFMLFAWML SRVLGASVVF RVGGWKCLKD VVVKFKKGAI
ESVSASEIKL SLRQSLVKLG VGFLSRDPKV QVLISDLEVV MRSSTSTTNL QKAKSHKPRT
SGRGKWMVVA NVARFLSVSV ADMVVKTTKV IVEVKELKLD INKDGGTKPN LYVKLNVLPI
LVHLCESRII SDQSSNVSFE CCPASQASSA SPDRSAATLF CDELSLSSEF GHDRAVGIVV
RNVEVTSGDV ILNFDEDSFP KSKQSSASLR SDEVRTSATA ASSAKKPHKE HQLVAALAKY
SSSFPEKVSF SLPKLDVRCV NREHDLLAEN NITGIQLRSV KSKSFEDTGE STRLDVQMEL
SEIHVFREAD SSILEIMKVD VVSFIYIPVQ PVLPIRAEVD IKLGGTRCNL FISRLQPWLR
LHFLKKKKLV LQEKTHNLEK TKAADMKAIM WTGTVSAPEM TVMLYGTEDI PLYHFCSQSS
HVFANNVSSL GTAVHVELGE LNLHLADEYQ ECFREHLFGI EPNSGSLMHI AKVSLDWGRR
DRTSSDEVGF RSKLVLSVDV TGMGIYFSFK RVQSLIINAL SFKALFKTLS VTGKKMNKTV
SVQPSKGSGK GTRLVNINLE RCCVNFCDDT GLDNTVIDDP KSVNYGSQGG RVSFSSLADG
TPRTASILST APEACKRLKY SVSLEISQFS FCLNKDKLST QMELGRAKSI YQEYLEEHTP
CSNVILFDMH NAKLVRRSGG LNEIDVCSLF SATHISLGWE PDVHLSFYEL FLRLRSLVYA
QRHKEPESGC NKGISSVKDG GPSEKINQSN SVNKQKKKES MFAIDVETLT ISAEVGDGVE
VKLEAQSIFS ENACIGVLLE GLMLAFNGSR VFKTTRMQVS RIPTATNLSD AVPVMTDGPW
DWVVQGLDVH ICMPYKLQLR AIDDSIEEML RGLKLISVAK GKHILSGKRE SSKPKKSSPK
FGRIKFCIRR LTADIEEEPI QGWLDEHYQL VKKEACELAV RLKFLEDLIH KAGQSPKGAE
TSAVLDERKM FFDGVEIDVE DPVAINKVKE EIHKRSFQSY YQACQGLAPS EGSGACREGF
QAGFKPSAAR TSLLSVCATD FDLSLTAVHG GDAGLIEVLK KLDPICEEND IPFSRLYGSN
VYLNTGSLVV QLRNYTLPLL SGTSGKCEGR IVLAQQATCF QPQISQDVFV GRWRKVKMFR
SASGTTPPLK TYSDLRIHFE QGEVSFGVGY EPAFADISYA FTVALRRANL SHRNPDMVQV
IKKERSLPWW DDMRNYVHGN ITLSFSESKW SVLATTDPYE SLDQLQIVSG PIELKQSDGR
VFVSAKDFKI KLSSLESLIS RHSLKVPVRA SGAAFIEAPD FNLEVTMDWD CESGNSLNHY
LYAFPAEGKP REKVFDPFRS TSLSLRWNFS LRPEKFHQSP SSTEHPTDVG TVYSSQDKPD
SIPLASPTMN LGAHDLAWIL KFWGLNYYPP HKLRSFSRWP RFGVPRAARS GNLSLDKVMT
EFMLRVDATP SLIKYMPWDS DDPAKGLTFN MAKLKYELCY SRGKQKYTFE CKRDALDLVY
QGLDLHVPKA FINKDEHPCI PGSVQVLRKS TQDALIDRVP SGKDHKRYEK HRDEGFLLSS
DYFTIRRQAP KADPERLLAW QEAGRRNLEM TYVRSEFENG SESDEHIRSD PSDDDGYNVV
IADNCQRVFV YGLKLLWTIE NRDAVWSFVG GISKAFEPPK PSPSRQYTQR KIHEENQKES
CPETHQGEMS RSSASPGRNL PSSPSHSIKI EKSDDIGTVE TIESEEEGTR HFMVNVIEPQ
FNLHSEEANG RFLLAAVSGR VLARSFHSIM RVGVEVIEQA LGTGSVKIPE CSPEMTWTRM
EVSVMLEHVQ AHVAPTDVDP GAGLQWLPKI RRNSPKVKRT GALLERVFMP CDMYFRYTRH
KGGTPDLKVK PLKELTFNSH NIIATMTSRQ FQVMLDVLTN LLFARLPKPR KSSLQCPTED
EDVEEEADEV VPYGVEEVEL AKINLEEKER ERKLLLDDIR KLSPCSDNMD DTHIEREGEL
WMISTRRSIL VQGLKKELTY AQKSRKAASA SLRMALQKAA QLRIMEKEKN KSPSYAMCIS
LQINKVVWSM LVDGKSFAEA EINDMIYDFD RDYKDIGVAR FTTKYFVVRN CLPNAKSDML
LSAWNPPPEW GKKVMLRVDA KQGAPKDAHY PLELFHVEIY PLRIHLTETM YRMMWEYFFP
EEEQDSQSRQ EVWKISTTAG SKRVKKGLVG HESSGHAIKD VEASRMSSSA LSASAAVQSQ
SNDDSVQKSN VICLRSSTGA SAQELRRTSS FDREENVAEP IANELVLQAH SCNVSSSIEQ
QEDFSKQKVK EIKPVKSGRS SHEEKKAGKS HEEKKSRPRK MMEFHNIKIS QVELLVTYEG
SRFVVNDLKL LMDTFHRVEF TGTWRRLFSR VKKHIIWGVL KSVTGMQGKK FKDKSHNNRE
STDNDLNLSD NDQTGKPDQQ QVTWFKRQSD GAGDGFVTSI RGLFNTQRRK AKAFVLRTMR
GEAENDFHGD WSDSDVEFSP FARQLTITKA KRLIRRHTKK FRPRSQRGST SQQRESLPSS
PIETTPFESG YSSGSSPYED FRE
