P06624 (MIP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lens fiber major intrinsic protein

Alternative name(s):
Aquaporin-0
MIP26
Short name=MP26

Gene names

Name:

MIP

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	263 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Ref.7
Subunit structure	Homotetramer. Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes. Ref.5 Ref.6 Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › gap junction.
Tissue specificity	Major component of lens fiber gap junctions.
Developmental stage	Higher expression in pre-natal (1-5 months gestation) than in postnatal (4-6 months) calf lens.
Domain	Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). Each tandem repeat contains a loop and a short helix that enter and leave the lipid bilayer on the same side.
Post-translational modification	Subject to partial proteolytic cleavage in the eye lens core. Partial proteolysis promotes interactions between tetramers from adjoining membranes By similarity.
Sequence similarities	Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell junction Cell membrane Gap junction Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Eye lens protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	gap junction Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	structural constituent of eye lens 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

Chain

1 – 263

263

Lens fiber major intrinsic protein

PRO_0000063910

Regions

Topological domain

1 – 8

8

Cytoplasmic Ref.5 Ref.6 Ref.7

Transmembrane

9 – 32

24

Helical

Topological domain

33 – 38

6

Extracellular Ref.5 Ref.6 Ref.7

Transmembrane

39 – 61

23

Helical

Intramembrane

62 – 67

6

Intramembrane

68 – 78

11

Helical

Topological domain

79 – 84

6

Cytoplasmic Ref.5 Ref.6 Ref.7

Transmembrane

85 – 107

23

Helical

Topological domain

108 – 126

19

Extracellular Ref.5 Ref.6 Ref.7

Transmembrane

127 – 147

21

Helical

Topological domain

148 – 159

12

Cytoplasmic Ref.5 Ref.6 Ref.7

Transmembrane

160 – 176

17

Helical

Intramembrane

177 – 183

7

Intramembrane

184 – 194

11

Helical

Topological domain

195 – 200

6

Extracellular Ref.5 Ref.6 Ref.7

Transmembrane

201 – 219

19

Helical

Topological domain

220 – 263

44

Cytoplasmic Ref.5 Ref.6 Ref.7

Motif

68 – 70

3

NPA 1

Motif

184 – 186

3

NPA 2

Amino acid modifications

Modified residue

235

1

Phosphoserine Ref.4

Modified residue

243

1

Phosphoserine; by PKA Ref.3

Modified residue

245

1

Phosphoserine Ref.3

Modified residue

246

1

Deamidated asparagine Ref.3

Experimental info

Sequence conflict

14

1

C → L AA sequence Ref.2

Sequence conflict

29 – 33

5

GASLR → RAFLL AA sequence Ref.2

Secondary structure

1

.

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.

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263

Helix Strand Turn

Details...

Helix

10 – 31

22

Helix

38 – 59

22

Turn

60 – 63

4

Helix

69 – 77

9

Helix

83 – 107

25

Turn

110 – 112

3

Turn

114 – 117

4

Helix

127 – 149

23

Helix

160 – 179

20

Helix

185 – 195

11

Turn

199 – 202

4

Helix

203 – 220

18

Turn

221 – 223

3

Helix

230 – 238

9

Beta strand

256 – 258

3

Sequences

	Sequence		Length	Mass (Da)
	P06624 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: E08C2C4F33398D4E	FASTA	263	28,223
	10 20 30 40 50 60 MWELRSASFW RAICAEFFAS LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALATLVQAVG 70 80 90 100 110 120 HISGAHVNPA VTFAFLVGSQ MSLLRAICYM VAQLLGAVAG AAVLYSVTPP AVRGNLALNT 130 140 150 160 170 180 LHPGVSVGQA TIVEIFLTLQ FVLCIFATYD ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG 190 200 210 220 230 240 AGMNPARSFA PAILTRNFTN HWVYWVGPVI GAGLGSLLYD FLLFPRLKSV SERLSILKGS 250 260 RPSESNGQPE VTGEPVELKT QAL

References

[1]	"The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning." Gorin M.B., Yancey S.B., Cline J., Revel J.-P., Horwitz J. Cell 39:49-59(1984) [PubMed: 6207938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-39.
[2]	"Sequence analysis of peptide fragments from the intrinsic membrane protein of calf lens fibers MP26 and its natural maturation product MP22." Ngoc L.D., Paroutaud P., Dunia I., Benedetti E.L., Hoebeke J. FEBS Lett. 181:74-78(1985) [PubMed: 3882455] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-33. Tissue: Lens.
[3]	"Amino acid sequence of in vivo phosphorylation sites in the main intrinsic protein (MIP) of lens membranes." Lampe P.D., Johnson R.G. Eur. J. Biochem. 194:541-547(1990) [PubMed: 2176601] [Abstract] Cited for: PROTEIN SEQUENCE OF 239-259, PHOSPHORYLATION AT SER-243 AND SER-245, DEAMIDATION AT ASN-246. Tissue: Lens.
[4]	"Complete map and identification of the phosphorylation site of bovine lens major intrinsic protein." Schey K.L., Fowler J.G., Schwartz J.C., Busman M., Dillon J., Crouch R.K. Invest. Ophthalmol. Vis. Sci. 38:2508-2515(1997) [PubMed: 9375569] [Abstract] Cited for: PHOSPHORYLATION AT SER-235. Tissue: Lens.
[5]	"The channel architecture of aquaporin 0 at a 2.2-A resolution." Harries W.E., Akhavan D., Miercke L.J., Khademi S., Stroud R.M. Proc. Natl. Acad. Sci. U.S.A. 101:14045-14050(2004) [PubMed: 15377788] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS), MEMBRANE TOPOLOGY, SUBUNIT.
[6]	"Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals." Palanivelu D.V., Kozono D.E., Engel A., Suda K., Lustig A., Agre P., Schirmer T. J. Mol. Biol. 355:605-611(2006) [PubMed: 16309700] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS), MEMBRANE TOPOLOGY, SUBUNIT.
[7]	"Lipid-protein interactions in double-layered two-dimensional AQP0 crystals." Gonen T., Cheng Y., Sliz P., Hiroaki Y., Fujiyoshi Y., Harrison S.C., Walz T. Nature 438:633-638(2005) [PubMed: 16319884] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, FUNCTION, MEMBRANE TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02818 mRNA. Translation: AAA30622.1.

IPI

IPI00699453.

PIR

MMBOLM. A23251.

RefSeq

NP_776362.1. NM_173937.1.

UniGene

Bt.4516.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YMG	X-ray	2.24	A	1-263	[»]
2B6O	X-ray	1.90	A	1-263	[»]
2B6P	X-ray	2.40	A	1-263	[»]
2C32	X-ray	7.01	A	1-263	[»]

ProteinModelPortal

P06624.

SMR

P06624. Positions 2-263.

ModBase

Search...

Protein-protein interaction databases

STRING

P06624.

Protein family/group databases

TCDB

1.A.8.8.2. major intrinsic protein (MIP) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000013360; ENSBTAP00000013360; ENSBTAG00000010127.

GeneID

280859.

KEGG

bta:280859.

Organism-specific databases

CTD

4284.

Phylogenomic databases

eggNOG

maNOG10666.

GeneTree

ENSGT00550000074347.

HOVERGEN

HBG000312.

InParanoid

P06624.

OMA

DSNGQPE.

OrthoDB

EOG4CJVHW.

PhylomeDB

P06624.

Family and domain databases

InterPro

IPR012269. Aquaporin.
IPR023271. Aquaporin-like.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]

Gene3D

G3DSA:1.20.1080.10. MIP. 1 hit.

KO

K09863.

PANTHER

PTHR19139. MIP. 1 hit.

Pfam

PF00230. MIP. 1 hit.
[Graphical view]

PRINTS

PR00783. MINTRINSICP.

SUPFAM

SSF81338. MIP. 1 hit.

TIGRFAMs

TIGR00861. MIP. 1 hit.

PROSITE

PS00221. MIP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MIP_BOVIN

Accession

Primary (citable) accession number: P06624

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program