ID   ANXA4_CANLF             Reviewed;         319 AA.
AC   P50994;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 123.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 79-96 AND 135-150,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Mongrel; 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).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-10.
RX   PubMed=7765250; DOI=10.1271/bbb.58.1282;
RA   Fukuoka S.;
RT   "Analysis of ZAPs, zymogen granule membrane associated proteins, in the
RT   regulated exocytosis of the pancreas.";
RL   Biosci. Biotechnol. Biochem. 58:1282-1285(1994).
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:0000269|PubMed:12020832}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:12020832}.
CC   -!- TISSUE SPECIFICITY: Expressed in pancreas (at protein level)
CC       (PubMed:12020832). Also detected in liver, spleen, intestine, stomach,
CC       kidney, and adrenal glands (PubMed:12020832).
CC       {ECO:0000269|PubMed:12020832}.
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; D38223; BAA07398.1; -; mRNA.
DR   PIR; PC2197; PC2197.
DR   AlphaFoldDB; P50994; -.
DR   SMR; P50994; -.
DR   STRING; 9615.ENSCAFP00000060866; -.
DR   PaxDb; P50994; -.
DR   PRIDE; P50994; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   InParanoid; P50994; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Cytoplasmic vesicle; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09525,
FT                   ECO:0000269|PubMed:7765250"
FT   CHAIN           2..319
FT                   /note="Annexin A4"
FT                   /id="PRO_0000067481"
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P09525"
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   CONFLICT        139
FT                   /note="V -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  35813 MW;  63C73B08EEA2AA81 CRC64;
     MAAKGGTVKP ASGFSATEDA QTLRKAMKGL GTDEDAIISV LAPRNTSQRQ EIRTAYKSTI
     GRDLMDDLKS ELSGNFERVI VGMITPTVLY DVQELRRAMK GSGTDEGCLI EILASRTPEE
     LRCINQTYQL QYGRSLEDVI RSDTSFMFQR VLVSLSAGGR DEGNFLDDAL MRQDAQDLYE
     AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRISQKDI EQGIKSETSG SFEDALLAIV
     KCMRNKSAYF AERLYKSMKG LGTDDNTLIR VMVSRAEIDM MDIRESFKRL YGKSLYSFIK
     GDTSGDYRKV LLILCGGDD