ID A0A2G9G7Q6_9LAMI Unreviewed; 253 AA.
AC A0A2G9G7Q6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Expansin {ECO:0000256|RuleBase:RU365023};
GN ORFNames=CDL12_26167 {ECO:0000313|EMBL:PIN01321.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN01321.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- FUNCTION: Causes 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.
CC {ECO:0000256|RuleBase:RU365023}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|RuleBase:RU365023}. Membrane
CC {ECO:0000256|RuleBase:RU365023}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365023}.
CC -!- SIMILARITY: Belongs to the expansin family. Expansin A subfamily.
CC {ECO:0000256|ARBA:ARBA00005392, ECO:0000256|RuleBase:RU365023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIN01321.1}.
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DR EMBL; NKXS01006474; PIN01321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9G7Q6; -.
DR STRING; 429701.A0A2G9G7Q6; -.
DR OrthoDB; 889108at2759; -.
DR Proteomes; UP000231279; 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:0009664; P:plant-type cell wall organization; IEA:InterPro.
DR CDD; cd22274; DPBB_EXPA_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; IPR002963; Expansin.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR007117; Expansin_CBD.
DR InterPro; IPR036749; Expansin_CBD_sf.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR31867; EXPANSIN-A15; 1.
DR PANTHER; PTHR31867:SF280; EXPANSIN-A8; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR Pfam; PF01357; Expansin_C; 1.
DR PRINTS; PR01226; EXPANSIN.
DR PRINTS; PR01225; EXPANSNFAMLY.
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 Cell wall {ECO:0000256|ARBA:ARBA00022512, ECO:0000256|RuleBase:RU365023};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|RuleBase:RU365023}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Secreted {ECO:0000256|RuleBase:RU365023};
KW Signal {ECO:0000256|RuleBase:RU365023}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT CHAIN 27..253
FT /note="Expansin"
FT /evidence="ECO:0000256|RuleBase:RU365023"
FT /id="PRO_5015212742"
FT DOMAIN 49..161
FT /note="Expansin-like EG45"
FT /evidence="ECO:0000259|PROSITE:PS50842"
FT DOMAIN 171..250
FT /note="Expansin-like CBD"
FT /evidence="ECO:0000259|PROSITE:PS50843"
SQ SEQUENCE 253 AA; 27108 MW; 7794C1B445EA4590 CRC64;
MYIPHLSMVS LVLFLFFGFF LSNAFGDYGG WDSAHATFYG GGDASGTMGG ACGYGNLYSQ
GYGTNTAALS TALFNNGLTC GACYELTCSG DPKWCLSGTI MVTATNFCPP NPSLPNDNGG
WCNPPRQHFD LAEPAFLQIA QYRAGIVPVS FRRVPCQKKG GIRFTINGHS YFNLVLVTNV
GGAGDVHSVS IKGSNTGWQP MSRNWGQNWQ SNSNINGQSL SFQVTTSDGR TVTSYNVAPA
GWQFGQTFEG GQF
//
