ANXA4_RAT
ID ANXA4_RAT Reviewed; 319 AA.
AC P55260;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Annexin A4;
DE AltName: Full=36 kDa zymogen granule membrane-associated protein;
DE Short=ZAP36;
DE AltName: Full=Annexin IV;
DE AltName: Full=Annexin-4;
DE AltName: Full=Lipocortin IV;
GN Name=Anxa4; Synonyms=Anx4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=12020832; DOI=10.1016/s0167-4781(02)00299-3;
RA Fukuoka S., Horst K., Kazuki-Sugino R., Ikeda Y.;
RT "Cloning and characterization of ZAP36, an annexin-like, zymogen granule
RT membrane associated protein, in exocrine pancreas.";
RL Biochim. Biophys. Acta 1575:148-152(2002).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P50994}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; D38224; BAA07399.2; -; mRNA.
DR PDB; 2ZHI; X-ray; 1.58 A; A=1-319.
DR PDB; 2ZHJ; X-ray; 1.35 A; A=1-319.
DR PDBsum; 2ZHI; -.
DR PDBsum; 2ZHJ; -.
DR AlphaFoldDB; P55260; -.
DR SMR; P55260; -.
DR STRING; 10116.ENSRNOP00000024436; -.
DR iPTMnet; P55260; -.
DR PhosphoSitePlus; P55260; -.
DR jPOST; P55260; -.
DR PaxDb; P55260; -.
DR PRIDE; P55260; -.
DR UCSC; RGD:621171; rat.
DR RGD; 621171; Anxa4.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P55260; -.
DR PhylomeDB; P55260; -.
DR EvolutionaryTrace; P55260; -.
DR PRO; PR:P55260; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; NAS:RGD.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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; IPR002391; ANX4.
DR PANTHER; PTHR10502:SF28; PTHR10502:SF28; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..319
FT /note="Annexin A4"
FT /id="PRO_0000067485"
FT REPEAT 14..85
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 86..157
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 169..241
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 245..316
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08132"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT MOD_RES 300
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:2ZHJ"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:2ZHJ"
SQ SEQUENCE 319 AA; 35849 MW; DE4B6A3F5B173005 CRC64;
METKGGTVKA ASGFNATEDA QVLRKAMKGL GTDEDAIIGV LACRNTAQRQ EIRTAYKSTI
GRDLLEDLKS ELSSNFEQVI LGMMTPTVLY DVQELRRAMK GAGTDEGCLI EILASRNPEE
IRRINQTYQQ QYGRSLEEDI CSDTSFMFQR VLVSLTAGGR DEGNYLDDAL VRQDAQDLYE
AGEKRWGTDE VKFLSILCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV
KCMRNKPAYF AERLYKSMKG LGTDDSTLIR VMVSRAEIDM LDIPANFKRV YGKSLYSFIK
GDTSGDYRKV LLILCGGDD
