Reviewed, UniProtKB/Swiss-Prot P13214 (ANXA4_BOVIN)

Names and origin

Protein names

Recommended name:
    Annexin A4
Alternative name(s):
    Annexin-4
    Annexin IV
    Lipocortin IV
    Endonexin I
    Chromobindin-4
    Protein II
    P32.5
    Placental anticoagulant protein II
      Short name=PAP-II
    PP4-X
    35-beta calcimedin
    Carbohydrate-binding protein p33/p41

Gene names

Name:	ANXA4
Synonyms:	ANX4

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A).
Subunit structure	Monomer. Binds to SFTPA1 in a Ca2+-dependent manner. Ref.5
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Miscellaneous	Seems to bind one calcium ion with high affinity.
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

Ontologies

Keywords
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 319

318

Annexin A4

PRO_0000067480

Regions

Repeat

23 – 83

61

Annexin 1

Repeat

95 – 155

61

Annexin 2

Repeat

179 – 239

61

Annexin 3

Repeat

254 – 314

61

Annexin 4

Amino acid modifications

Modified residue

165

1

Phosphotyrosine By similarity

Modified residue

213

1

N6-acetyllysine By similarity

Modified residue

225

1

N6-acetyllysine By similarity

Modified residue

293

1

N6-acetyllysine By similarity

Modified residue

300

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

95

1

L → V in BAA11243. Ref.2

Sequence conflict

198

1

C → Y AA sequence Ref.4

Sequence conflict

211

1

E → K in BAA11243. Ref.2

Secondary structure

1

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319

Helix Strand Turn

Details...

Helix

16 – 27

12

Beta strand

28 – 31

4

Helix

34 – 41

8

Helix

46 – 60

15

Helix

64 – 71

8

Helix

74 – 84

11

Helix

87 – 99

13

Beta strand

100 – 103

4

Helix

106 – 115

10

Helix

118 – 132

15

Helix

136 – 143

8

Helix

146 – 156

11

Helix

168 – 183

16

Turn

184 – 186

3

Helix

190 – 199

10

Helix

202 – 216

15

Helix

220 – 227

8

Helix

230 – 258

29

Beta strand

259 – 262

4

Helix

265 – 275

11

Turn

276 – 278

3

Helix

280 – 291

12

Helix

295 – 302

8

Helix

305 – 315

11

Sequences

	Sequence		Length	Mass (Da)
	P13214-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A795DD72B0EE961F	FASTA	319	35,889
	10 20 30 40 50 60 MAAKGGTVKA ASGFNAAEDA QTLRKAMKGL GTDEDAIINV LAYRSTAQRQ EIRTAYKTTI 70 80 90 100 110 120 GRDLMDDLKS ELSGNFEQVI LGMMTPTVLY DVQELRKAMK GAGTDEGCLI EILASRTPEE 130 140 150 160 170 180 IRRINQTYQL QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DESNYLDDAL MRQDAQDLYE 190 200 210 220 230 240 AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRIAQKDI EQSIKSETSG SFEDALLAIV 250 260 270 280 290 300 KCMRNKSAYF AERLYKSMKG LGTDDDTLIR VMVSRAEIDM LDIRANFKRL YGKSLYSFIK 310 GDTSGDYRKV LLILCGGDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a cDNA encoding bovine endonexin (chromobindin 4)." Hamman H.C., Gaffey L.C., Lynch K.R., Creutz C.E. Biochem. Biophys. Res. Commun. 156:660-667(1988) [PubMed: 2847715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Characterization of carbohydrate-binding protein p33/41: relation with annexin IV, molecular basis of the doublet forms (p33 and p41), and modulation of the carbohydrate binding activity by phospholipids." Kojima K., Yamamoto K., Irimura T., Osawa T., Ogawa H., Matsumoto I. J. Biol. Chem. 271:7679-7685(1996) [PubMed: 8631806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[4]	"Carbohydrate-binding proteins in bovine kidney have consensus amino acid sequences of annexin family proteins." Kojima K., Ogawa H.K., Seno N., Yamamoto K., Irimura T., Osawa T., Matsumoto I. J. Biol. Chem. 267:20536-20539(1992) [PubMed: 1400371] [Abstract] Cited for: PROTEIN SEQUENCE OF 10-24; 28-48; 101-118; 194-212 AND 260-288. Tissue: Kidney.
[5]	"Ca(2+)-dependent binding of annexin IV to surfactant protein A and lamellar bodies in alveolar type II cells." Sohma H., Matsushima N., Watanabe T., Hattori A., Kuroki Y., Akino T. Biochem. J. 312:175-181(1995) [PubMed: 7492310] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-44; 111-118; 162-190 AND 226-235, INTERACTION WITH SFTPA1.
[6]	Sutton R.B., Sprang S.R. Submitted (SEP-1995) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[7]	"Structure of the trigonal crystal form of bovine annexin IV." Zanotti G., Malpeli G., Gliubich F., Folli C., Stoppini M., Olivi L., Savoia A., Berni R. Biochem. J. 329:101-106(1998) [PubMed: 9405281] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22248 mRNA. Translation: AAA30507.1.
X13627 mRNA. Translation: CAA31954.1.
D78178 mRNA. Translation: BAA11243.1.
BC103381 mRNA. Translation: AAI03382.1.

IPI

IPI00686981.

PIR

LUBO4. A31578.

RefSeq

NP_001001440.2.

UniGene

Bt.38197

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ANN	X-ray	2.30	A	2-318	[»]
1AOW	X-ray	3.00	A	11-319	[»]
1I4A	X-ray	2.00	A	2-318	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P13214.

Genome annotation databases

Ensembl

ENSBTAT00000001463; ENSBTAP00000001463; ENSBTAG00000001105; Bos taurus. [Genome view]

GeneID

281625.

KEGG

bta:281625.

Organism-specific databases

CTD

281625.

Phylogenomic databases

eggNOG

maNOG13619.

HOVERGEN

P13214.

InParanoid

P13214.

OMA

AEIDMLD.

OrthoDB

EOG9TF34M.

PhylomeDB

P13214.

Family and domain databases

InterPro

IPR001464. Annexin.
IPR015474. Annexin_IV.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
[Graphical view]

Gene3D

G3DSA:1.10.220.10. Annexin. 4 hits.

PANTHER

PTHR10502. Annexin. 1 hit.
PTHR10502:SF28. Annexin_IV. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.

SMART

SM00335. ANX. 4 hits.
[Graphical view]

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ANXA4_BOVIN

Accession

Primary (citable) accession number: P13214
Secondary accession number(s): Q3SYU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)