BRYP_PHYPA
ID BRYP_PHYPA Reviewed; 178 AA.
AC Q5UCA8; A9TTZ8;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Bryoporin {ECO:0000303|PubMed:19674339};
DE Short=PpBP {ECO:0000303|PubMed:19674339};
DE AltName: Full=Physcomitrin {ECO:0000303|Ref.2};
GN ORFNames=PHYPADRAFT_61094 {ECO:0000312|EMBL:EDQ53098.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shin J.S., Hoang Q.T., Cho S.H.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shin J.S., Hoang Q.T., Cho S.H.;
RT "A Novel Cytolysin of Physcomitrella patens, Physcomitrin.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, 3D-STRUCTURE MODELING, AND
RP ACTIVITY REGULATION.
RX PubMed=19674339; DOI=10.1111/j.1469-8137.2009.02975.x;
RA Hoang Q.T., Cho S.H., McDaniel S.F., Ok S.H., Quatrano R.S., Shin J.S.;
RT "An actinoporin plays a key role in water stress in the moss Physcomitrella
RT patens.";
RL New Phytol. 184:502-510(2009).
CC -!- FUNCTION: Actinoporin-related protein having hemolytic activity in
CC vitro. Binds probably a phosphocholine derivative with the unique amido
CC or hydroxyl groups found in sphingomyelin. Involved in drought
CC tolerance. {ECO:0000269|PubMed:19674339}.
CC -!- ACTIVITY REGULATION: Inhibited by sphingomyelin.
CC {ECO:0000269|PubMed:19674339}.
CC -!- DEVELOPMENTAL STAGE: Very low expression in protonema. Expressed in
CC gametophores, with a maximal level in mature gametophores.
CC {ECO:0000269|PubMed:19674339}.
CC -!- INDUCTION: Strongly up-regulated by abscisic acid, osmotic stress and
CC drought, up-regulated by wounding, jasmonic acid or salicylic acid and
CC not induced by salt, cold or auxins. {ECO:0000269|PubMed:19674339}.
CC -!- DOMAIN: The Trp-rich region is important for the binding to lipid
CC membrane. {ECO:0000250|UniProtKB:P61914}.
CC -!- SIMILARITY: Belongs to the actinoporin family. Plant subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDQ53098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY762377; AAV41095.2; -; mRNA.
DR EMBL; AY772731; AAV65396.1; -; Genomic_DNA.
DR EMBL; DS545208; EDQ53098.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001782104.1; XM_001782052.1.
DR AlphaFoldDB; Q5UCA8; -.
DR SMR; Q5UCA8; -.
DR STRING; 3218.PP1S319_5V6.1; -.
DR EnsemblPlants; Pp3c23_22700V3.2; Pp3c23_22700V3.2; Pp3c23_22700.
DR Gramene; Pp3c23_22700V3.2; Pp3c23_22700V3.2; Pp3c23_22700.
DR eggNOG; ENOG502SGU7; Eukaryota.
DR Proteomes; UP000006727; Chromosome 23.
DR GO; GO:0046930; C:pore complex; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0006812; P:cation transport; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0046931; P:pore complex assembly; IEA:InterPro.
DR Gene3D; 2.60.270.20; -; 1.
DR InterPro; IPR009104; Anemon_actinoporin-like.
DR InterPro; IPR015926; Cytolysin/lectin.
DR Pfam; PF06369; Anemone_cytotox; 1.
DR SUPFAM; SSF63724; SSF63724; 1.
PE 2: Evidence at transcript level;
KW Cytolysis; Hemolysis; Reference proteome; Stress response.
FT CHAIN 1..178
FT /note="Bryoporin"
FT /id="PRO_0000434639"
FT REGION 101..117
FT /note="Trp-rich region"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 51
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 83
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 102
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 104
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
FT BINDING 134
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000250|UniProtKB:P07845"
SQ SEQUENCE 178 AA; 19877 MW; 1E30CFE10AF33A50 CRC64;
MAEAIIPAAE LSIKTLQNIV EGITGVDRKI AIGFKNLTDY TLENLGVYFN SGSSDRSIAY
KINAQEALLF SARKSDHTAR GTVGTFSYYI QDEDKTVHVM WSVPFDYNLY SNWWNIAVVD
GRQPPDSNVH DNLYNGSGGM PYPNKPDQYI NNEQKGFHLF GSMTNNGQAT IEVELKKA
