ANX1_GOSHI
ID ANX1_GOSHI Reviewed; 315 AA.
AC P93157;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Annexin Gh1 {ECO:0000303|PubMed:12787021, ECO:0000303|PubMed:16331990, ECO:0000303|PubMed:18441010};
DE Short=Anx(Gh1) {ECO:0000303|PubMed:12142457, ECO:0000303|PubMed:12787021};
DE Flags: Fragment;
GN Name=AnnGh1 {ECO:0000303|PubMed:9230934, ECO:0000312|EMBL:AAB67993.2};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000312|EMBL:AAB67993.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Acala SJ2 {ECO:0000303|Ref.1}; TISSUE=Fiber {ECO:0000303|Ref.1};
RA Potikha T.S., Delmer D.P.;
RT "cDNA Clones for Annexin AnnGh1 (Accession No. U73746) and AnnGh2
RT (Accession No. U73747) from Gossypium hirsutum (cotton)1 (PGR97-003).";
RL Plant Physiol. 113:305-305(1997).
RN [2] {ECO:0000312|EMBL:AAB67993.2}
RP GENE NAME.
RX PubMed=9230934; DOI=10.1007/s000180050070;
RA Delmer D.P., Potikha T.S.;
RT "Structures and functions of annexins in plants.";
RL Cell. Mol. Life Sci. 53:546-553(1997).
RN [3]
RP SUBUNIT.
RX PubMed=12142457; DOI=10.1110/ps.4770102;
RA Hofmann A., Ruvinov S., Hess S., Schantz R., Delmer D.P., Wlodawer A.;
RT "Plant annexins form calcium-independent oligomers in solution.";
RL Protein Sci. 11:2033-2040(2002).
RN [4]
RP FUNCTION.
RX PubMed=16331990; DOI=10.1021/bi0516226;
RA Dabitz N., Hu N.J., Yusof A.M., Tranter N., Winter A., Daley M.,
RA Zschoernig O., Brisson A., Hofmann A.;
RT "Structural determinants for plant annexin-membrane interactions.";
RL Biochemistry 44:16292-16300(2005).
RN [5] {ECO:0007744|PDB:1N00}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=12787021; DOI=10.1046/j.1432-1033.2003.03612.x;
RA Hofmann A., Delmer D.P., Wlodawer A.;
RT "The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an
RT unusual S3 cluster.";
RL Eur. J. Biochem. 270:2557-2564(2003).
RN [6] {ECO:0007744|PDB:3BRX}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION,
RP AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=18441010; DOI=10.1074/jbc.m801051200;
RA Hu N.J., Yusof A.M., Winter A., Osman A., Reeve A.K., Hofmann A.;
RT "The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum
RT and its implications for membrane binding mechanisms of plant annexins.";
RL J. Biol. Chem. 283:18314-18322(2008).
CC -!- FUNCTION: Binds to phospholipid vesicles in a calcium-dependent manner
CC in vitro (PubMed:16331990, PubMed:18441010). Prefers phosphatidyl-
CC serine containing membranes. May have a role in the membrane
CC cytoskeleton scaffolding or exocytotic processes (PubMed:16331990). May
CC be involved in oxidative stress response (Probable).
CC {ECO:0000269|PubMed:16331990, ECO:0000269|PubMed:18441010,
CC ECO:0000305|PubMed:12787021}.
CC -!- SUBUNIT: Monomer (PubMed:12142457, PubMed:12787021). Trimer.
CC Oligomerization is calcium-independent. Disassembly of the oligomers
CC seems to be required for calcium-binding (PubMed:12787021).
CC {ECO:0000269|PubMed:12142457, ECO:0000269|PubMed:12787021}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:16331990,
CC ECO:0000305|PubMed:18441010}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid. {ECO:0000255|RuleBase:RU003540}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000255|RuleBase:RU003540}.
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DR EMBL; U73746; AAB67993.2; -; mRNA.
DR PIR; T10805; T10805.
DR PDB; 1N00; X-ray; 2.10 A; A=1-315.
DR PDB; 3BRX; X-ray; 2.50 A; A=1-315.
DR PDBsum; 1N00; -.
DR PDBsum; 3BRX; -.
DR AlphaFoldDB; P93157; -.
DR SMR; P93157; -.
DR EvolutionaryTrace; P93157; -.
DR Proteomes; UP000189702; Genome assembly.
DR GO; GO:0070382; C:exocytic vesicle; IC:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISM:AgBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:AgBase.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IC:UniProtKB.
DR GO; GO:0009835; P:fruit ripening; TAS:AgBase.
DR GO; GO:0070206; P:protein trimerization; IDA:UniProtKB.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; TAS:AgBase.
DR GO; GO:0006979; P:response to oxidative stress; TAS:AgBase.
DR GO; GO:0032940; P:secretion by cell; TAS:AgBase.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR009118; AnnexinD_plant.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01814; ANNEXINPLANT.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Annexin; Calcium; Calcium/phospholipid-binding; Membrane;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN <1..315
FT /note="Annexin Gh1"
FT /id="PRO_0000450599"
FT REPEAT 10..81
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 82..153
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 165..236
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 240..311
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18441010,
FT ECO:0007744|PDB:3BRX"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAB67993.2"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1N00"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:1N00"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:1N00"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3BRX"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:1N00"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1N00"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:1N00"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1N00"
SQ SEQUENCE 315 AA; 35824 MW; 653113C77AAAE980 CRC64;
ATLTVPTTVP SVSEDCEQLR KAFSGWGTNE GLIIDILGHR NAEQRNLIRK TYAETYGEDL
LKALDKELSN DFERLVLLWA LDPAERDALL ANEATKRWTS SNQVLMEIAC TRSANQLLHA
RQAYHARYKK SLEEDVAHHT TGDFHKLLLP LVSSYRYEGE EVNMTLAKTE AKLLHEKISN
KAYSDDDVIR VLATRSKAQI NATLNHYKNE YGNDINKDLK ADPKDEFLAL LRSTVKCLVY
PEKYFEKVLR LAINRRGTDE GALTRVVCTR AEVDLKVIAD EYQRRNSVPL TRAIVKDTHG
DYEKLLLVLA GHVEN
