ANXA4_BOVIN
ID ANXA4_BOVIN Reviewed; 319 AA.
AC P13214; Q3SYU5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Annexin A4;
DE AltName: Full=35-beta calcimedin;
DE AltName: Full=Annexin IV;
DE AltName: Full=Annexin-4;
DE AltName: Full=Carbohydrate-binding protein p33/p41;
DE AltName: Full=Chromobindin-4;
DE AltName: Full=Endonexin I;
DE AltName: Full=Lipocortin IV;
DE AltName: Full=P32.5;
DE AltName: Full=PP4-X;
DE AltName: Full=Placental anticoagulant protein II;
DE Short=PAP-II;
DE AltName: Full=Protein II;
GN Name=ANXA4; Synonyms=ANX4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2847715; DOI=10.1016/s0006-291x(88)80893-3;
RA Hamman H.C., Gaffey L.C., Lynch K.R., Creutz C.E.;
RT "Cloning and characterization of a cDNA encoding bovine endonexin
RT (chromobindin 4).";
RL Biochem. Biophys. Res. Commun. 156:660-667(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8631806; DOI=10.1074/jbc.271.13.7679;
RA Kojima K., Yamamoto K., Irimura T., Osawa T., Ogawa H., Matsumoto I.;
RT "Characterization of carbohydrate-binding protein p33/41: relation with
RT annexin IV, molecular basis of the doublet forms (p33 and p41), and
RT modulation of the carbohydrate binding activity by phospholipids.";
RL J. Biol. Chem. 271:7679-7685(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 10-24; 28-48; 101-118; 194-212 AND 260-288.
RC TISSUE=Kidney;
RX PubMed=1400371; DOI=10.1016/s0021-9258(19)36715-8;
RA Kojima K., Ogawa H.K., Seno N., Yamamoto K., Irimura T., Osawa T.,
RA Matsumoto I.;
RT "Carbohydrate-binding proteins in bovine kidney have consensus amino acid
RT sequences of annexin family proteins.";
RL J. Biol. Chem. 267:20536-20539(1992).
RN [5]
RP PROTEIN SEQUENCE OF 29-44; 111-118; 162-190 AND 226-235, AND INTERACTION
RP WITH SFTPA1.
RX PubMed=7492310; DOI=10.1042/bj3120175;
RA Sohma H., Matsushima N., Watanabe T., Hattori A., Kuroki Y., Akino T.;
RT "Ca(2+)-dependent binding of annexin IV to surfactant protein A and
RT lamellar bodies in alveolar type II cells.";
RL Biochem. J. 312:175-181(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RA Sutton R.B., Sprang S.R.;
RL Submitted (SEP-1995) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=9405281; DOI=10.1042/bj3290101;
RA Zanotti G., Malpeli G., Gliubich F., Folli C., Stoppini M., Olivi L.,
RA Savoia A., Berni R.;
RT "Structure of the trigonal crystal form of bovine annexin IV.";
RL Biochem. J. 329:101-106(1998).
CC -!- FUNCTION: May play a role in alveolar type II cells through interaction
CC with the surfactant protein SFTPA1 (SP-A).
CC -!- SUBUNIT: Monomer. Binds to SFTPA1 in a Ca(2+)-dependent manner.
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 -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; M22248; AAA30507.1; -; mRNA.
DR EMBL; X13627; CAA31954.1; -; mRNA.
DR EMBL; D78178; BAA11243.1; -; mRNA.
DR EMBL; BC103381; AAI03382.1; -; mRNA.
DR PIR; A31578; LUBO4.
DR RefSeq; NP_001001440.2; NM_001001440.2.
DR PDB; 1ANN; X-ray; 2.30 A; A=2-319.
DR PDB; 1AOW; X-ray; 3.00 A; A=11-319.
DR PDB; 1I4A; X-ray; 2.00 A; A=2-319.
DR PDBsum; 1ANN; -.
DR PDBsum; 1AOW; -.
DR PDBsum; 1I4A; -.
DR AlphaFoldDB; P13214; -.
DR SMR; P13214; -.
DR STRING; 9913.ENSBTAP00000001463; -.
DR ChEMBL; CHEMBL3308973; -.
DR PaxDb; P13214; -.
DR PeptideAtlas; P13214; -.
DR PRIDE; P13214; -.
DR Ensembl; ENSBTAT00000001463; ENSBTAP00000001463; ENSBTAG00000001105.
DR GeneID; 281625; -.
DR KEGG; bta:281625; -.
DR CTD; 307; -.
DR VEuPathDB; HostDB:ENSBTAG00000001105; -.
DR VGNC; VGNC:25966; ANXA4.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000156575; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P13214; -.
DR OMA; RHFMIVL; -.
DR OrthoDB; 856254at2759; -.
DR TreeFam; TF105452; -.
DR EvolutionaryTrace; P13214; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000001105; Expressed in urinary bladder and 108 other tissues.
DR ExpressionAtlas; P13214; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; TAS:AgBase.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042584; C:chromaffin granule membrane; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; TAS:AgBase.
DR GO; GO:0035374; F:chondroitin sulfate binding; IDA:AgBase.
DR GO; GO:0008201; F:heparin binding; IDA:AgBase.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
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; Direct protein sequencing; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09525"
FT CHAIN 2..319
FT /note="Annexin A4"
FT /id="PRO_0000067480"
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 95
FT /note="L -> V (in Ref. 2; BAA11243)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="C -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="E -> K (in Ref. 2; BAA11243)"
FT /evidence="ECO:0000305"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1I4A"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1I4A"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:1I4A"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1ANN"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 230..258
FT /evidence="ECO:0007829|PDB:1I4A"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:1I4A"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:1I4A"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:1I4A"
SQ SEQUENCE 319 AA; 35889 MW; A795DD72B0EE961F CRC64;
MAAKGGTVKA ASGFNAAEDA QTLRKAMKGL GTDEDAIINV LAYRSTAQRQ EIRTAYKTTI
GRDLMDDLKS ELSGNFEQVI LGMMTPTVLY DVQELRKAMK GAGTDEGCLI EILASRTPEE
IRRINQTYQL QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DESNYLDDAL MRQDAQDLYE
AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRIAQKDI EQSIKSETSG SFEDALLAIV
KCMRNKSAYF AERLYKSMKG LGTDDDTLIR VMVSRAEIDM LDIRANFKRL YGKSLYSFIK
GDTSGDYRKV LLILCGGDD
