ANX12_HYDVU
ID ANX12_HYDVU Reviewed; 316 AA.
AC P26256;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Annexin-B12;
DE AltName: Full=Annexin XII;
DE AltName: Full=Annexin-12;
GN Name=ANXB12;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1339458; DOI=10.1016/s0021-9258(19)50123-5;
RA Schlaepfer D.D., Fisher D.A., Brandt M.E., Bode H.R., Jones J.M.,
RA Haigler H.T.;
RT "Identification of a novel annexin in Hydra vulgaris. Characterization,
RT cDNA cloning, and protein kinase C phosphorylation of annexin XII.";
RL J. Biol. Chem. 267:9529-9539(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7477411; DOI=10.1038/378512a0;
RA Luecke H., Chang B.T., Maillard W.S., Schlaepfer D.D., Haigler H.T.;
RT "Crystal structure of the annexin XII hexamer and implications for bilayer
RT insertion.";
RL Nature 378:512-515(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF MUTANT LYS-105.
RX PubMed=10704197; DOI=10.1021/bi992278d;
RA Cartailler J.-P., Haigler H.T., Luecke H.;
RT "Annexin XII E105K crystal structure: identification of a pH-dependent
RT switch for mutant hexamerization.";
RL Biochemistry 39:2475-2483(2000).
CC -!- SUBUNIT: Homohexamer.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- PTM: Phosphorylated in vitro on serine(s) and threonine(s) by PKC.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; M83736; AAA29206.1; -; mRNA.
DR PIR; A42660; LUJF12.
DR RefSeq; NP_001296699.1; NM_001309770.1.
DR RefSeq; XP_002155286.3; XM_002155250.3.
DR PDB; 1AEI; X-ray; 2.80 A; A/B/C/D/E/F=2-316.
DR PDB; 1DM5; X-ray; 1.93 A; A/B/C/D/E/F=2-316.
DR PDBsum; 1AEI; -.
DR PDBsum; 1DM5; -.
DR AlphaFoldDB; P26256; -.
DR SMR; P26256; -.
DR TCDB; 1.A.31.1.9; the annexin (annexin) family.
DR PRIDE; P26256; -.
DR GeneID; 100203975; -.
DR KEGG; hmg:100203975; -.
DR OMA; KEEYRAM; -.
DR OrthoDB; 856254at2759; -.
DR EvolutionaryTrace; P26256; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
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 Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 3.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Annexin; Calcium; Calcium/phospholipid-binding;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..316
FT /note="Annexin-B12"
FT /id="PRO_0000067519"
FT REPEAT 13..84
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 85..156
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 168..240
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 244..315
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 6
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:1DM5"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1DM5"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:1DM5"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1DM5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 201..214
FT /evidence="ECO:0007829|PDB:1DM5"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 229..257
FT /evidence="ECO:0007829|PDB:1DM5"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1AEI"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:1DM5"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:1DM5"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1DM5"
SQ SEQUENCE 316 AA; 35109 MW; 10599869CBA853EC CRC64;
MVVQGTVKPH ASFNSREDAE TLRKAMKGIG TDEKSITHIL ATRSNAQRQQ IKTDYTTLFG
KHLEDELKSE LSGNYEAAAL ALLRKPDEFL AEQLHAAMKG LGTDENALID ILCTQSNAQI
HAIKAAFKLL YKEDLEKEII SETSGNFQRL LVSMLQGGRK EDEPVNAAHA AEDAAAIYQA
GEGQIGTDES RFNAVLATRS YPQLHQIFHE YSKISNKTIL QAIENEFSGD IKNGLLAIVK
SVENRFAYFA ERLHHAMKGL GTSDKTLIRI LVSRSEIDLA NIKETFQAMY GKSLYEFIAD
DCSGDYKDLL LQITGH
