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HLB1_ARATH
ID   HLB1_ARATH              Reviewed;         565 AA.
AC   Q9FHY8;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=Protein HLB1 {ECO:0000303|PubMed:26941089};
DE   AltName: Full=HYPERSENSITIVE TO LATRUNCULIN B1 {ECO:0000303|PubMed:26941089};
GN   Name=HLB1 {ECO:0000303|PubMed:26941089};
GN   OrderedLocusNames=At5g41950 {ECO:0000312|Araport:AT5G41950};
GN   ORFNames=MJC20.5 {ECO:0000312|EMBL:AED94746.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(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].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, 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   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DOMAIN, AND
RP   INTERACTION WITH BIG5.
RX   PubMed=26941089; DOI=10.1105/tpc.15.00794;
RA   Sparks J.A., Kwon T., Renna L., Liao F., Brandizzi F., Blancaflor E.B.;
RT   "HLB1 is a tetratricopeptide repeat domain-containing protein that operates
RT   at the intersection of the exocytic and endocytic pathways at the TGN/EE in
RT   Arabidopsis.";
RL   Plant Cell 28:746-769(2016).
CC   -!- FUNCTION: Component of the endomembrane trafficking machinery that is
CC       involved in protein recycling to the plasma membrane. Forms a complex
CC       with BIG5/MIN7/BEN1 and actin to modulate the function of the trans-
CC       Golgi network /early endosome at the intersection of the exocytic and
CC       endocytic pathways. May be linking post-Golgi traffic with the actin
CC       cytoskeleton. {ECO:0000269|PubMed:26941089}.
CC   -!- SUBUNIT: Interacts with BIG5. {ECO:0000269|PubMed:26941089}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26941089}.
CC       Endomembrane system {ECO:0000269|PubMed:26941089}. Golgi apparatus,
CC       trans-Golgi network {ECO:0000269|PubMed:26941089}. Early endosome
CC       {ECO:0000269|PubMed:26941089}.
CC   -!- DOMAIN: The C-terminal domain (496-565) is responsible for the
CC       localization to the trans-Golgi network/early endosome.
CC       {ECO:0000269|PubMed:26941089}.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitivity to latrunculin B1 (LatB) and
CC       cytochalasin, reduced primary root length and root hair growth defects.
CC       {ECO:0000269|PubMed:26941089}.
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DR   EMBL; AB017067; BAB08428.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94746.1; -; Genomic_DNA.
DR   EMBL; AY128348; AAM91551.1; -; mRNA.
DR   EMBL; BT030345; ABO38758.1; -; mRNA.
DR   EMBL; AY085561; AAM62783.1; -; mRNA.
DR   RefSeq; NP_199010.1; NM_123560.4.
DR   AlphaFoldDB; Q9FHY8; -.
DR   SMR; Q9FHY8; -.
DR   STRING; 3702.AT5G41950.1; -.
DR   iPTMnet; Q9FHY8; -.
DR   MetOSite; Q9FHY8; -.
DR   PaxDb; Q9FHY8; -.
DR   PRIDE; Q9FHY8; -.
DR   ProMEX; Q9FHY8; -.
DR   ProteomicsDB; 230228; -.
DR   EnsemblPlants; AT5G41950.1; AT5G41950.1; AT5G41950.
DR   GeneID; 834200; -.
DR   Gramene; AT5G41950.1; AT5G41950.1; AT5G41950.
DR   KEGG; ath:AT5G41950; -.
DR   Araport; AT5G41950; -.
DR   TAIR; locus:2165725; AT5G41950.
DR   eggNOG; ENOG502QR9B; Eukaryota.
DR   HOGENOM; CLU_034799_0_0_1; -.
DR   InParanoid; Q9FHY8; -.
DR   OMA; TIAPHKH; -.
DR   OrthoDB; 671340at2759; -.
DR   PhylomeDB; Q9FHY8; -.
DR   PRO; PR:Q9FHY8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHY8; baseline and differential.
DR   GO; GO:0005769; C:early endosome; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR   GO; GO:0006887; P:exocytosis; IMP:TAIR.
DR   GO; GO:0080147; P:root hair cell development; IMP:TAIR.
DR   GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR   GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:TAIR.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..565
FT                   /note="Protein HLB1"
FT                   /id="PRO_0000440018"
FT   REPEAT          189..222
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          237..270
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          282..315
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          326..359
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          361..391
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          392..425
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   565 AA;  62398 MW;  B7A575D4E00BA608 CRC64;
     MADTVEEPQL QNGAAPAESE TEQNPIPEPQ LQTEPKLTGE IPEIEADLTP EEVQSEVTDA
     KPEEVQSEVK PEEVKTVVTD AKPEEAQSEV KPEEVQSVVT DTKPDLTDVD LSPGGSEEIP
     IRSTEVEQES TTSVLKKDDD GNKTFTMREL LSELKSEEGD GTPHSSASPF SRESASQPAE
     NNPAMDLINR IQVNDEEGRS RQRVLAFAAR KYASAIERNP DDHDALYNWA LILQESADNV
     SPDSVSPSKD DLLEEACKKY DEATRLCPTL YDAYYNWAIA ISDRAKIRGR TKEAEELWEQ
     AADNYEKAVQ LNWNSSQALN NWGLVLQELS QIVPAREKEK VVRTAISKFR AAIRLQFDFH
     RAIYNLGTVL YGLAEDTLRT GGSGNGKDMP PGELYSQSAI YIAAAHSLKP SYSVYSSALR
     LVRSMLPLPH LKVGYLTAPP VGNSLAPHSD WKRTEFELNH ERLLQVLKPE PREMGRNLSG
     KAETMSTNVE RKTVKVNITE IVSVTPCADL TLPPGAGLCI DTIHGPVFLV ADSWESLDGW
     LDAIRLVYTI YARGKSDVLA GIITG
 
 
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