ID I1QVP8_ORYGL Unreviewed; 269 AA.
AC I1QVP8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Expansin-like EG45 domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA10G0128100.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA10G0128100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: May cause loosening and extension of plant cell walls by
CC disrupting non-covalent bonding between cellulose microfibrils and
CC matrix glucans. No enzymatic activity has been found. May be required
CC for rapid internodal elongation in deepwater rice during submergence.
CC {ECO:0000256|ARBA:ARBA00025488}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Secreted,
CC cell wall {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the expansin family. Expansin B subfamily.
CC {ECO:0000256|ARBA:ARBA00005650}.
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DR AlphaFoldDB; I1QVP8; -.
DR STRING; 4538.I1QVP8; -.
DR EnsemblPlants; ORGLA10G0128100.1; ORGLA10G0128100.1; ORGLA10G0128100.
DR Gramene; ORGLA10G0128100.1; ORGLA10G0128100.1; ORGLA10G0128100.
DR eggNOG; ENOG502QRTE; Eukaryota.
DR HOGENOM; CLU_027462_1_0_1; -.
DR OMA; TWYGQPY; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR CDD; cd22275; DPBB_EXPB_N; 1.
DR Gene3D; 2.60.40.760; Expansin, cellulose-binding-like domain; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR007118; Expan_Lol_pI.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR007117; Expansin_CBD.
DR InterPro; IPR036749; Expansin_CBD_sf.
DR InterPro; IPR005795; LolPI.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR31692; EXPANSIN-B3; 1.
DR PANTHER; PTHR31692:SF7; EXPANSIN-B9; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR Pfam; PF01357; Expansin_C; 1.
DR PRINTS; PR01225; EXPANSNFAMLY.
DR PRINTS; PR00829; LOLP1ALLERGN.
DR SMART; SM00837; DPBB_1; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR SUPFAM; SSF49590; PHL pollen allergen; 1.
DR PROSITE; PS50843; EXPANSIN_CBD; 1.
DR PROSITE; PS50842; EXPANSIN_EG45; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..269
FT /note="Expansin-like EG45 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003651804"
FT DOMAIN 63..169
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT DOMAIN 183..264
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000259|PROSITE:PS50843"
SQ SEQUENCE 269 AA; 28981 MW; 5CEF355E64938037 CRC64;
MGSLTTNIVL AVAVVAALVG GGSCGPPKVP PGPNITTNYN APWLPARATW YGQPYGSGPA
DNGGACGIKN VNLPPYNGMI SCGNVPIFKD GRGCGSCYEV KCEQPAACSK QPVTVFITDM
NYEPISAYHF DFSGKAFGAM ACPGKETELR KAGIIDMQFR RVRCKYPSGQ KVTFHVEKGS
NPNYLAVLVK FVADDGDVIQ MDLQEAGLPA WRPMKLSWGA IWRMDTATPL KAPFSIRVTT
ESGKSLIAKD VIPVNWMPDA VYVSNVQFY
//
