Q6RZ07 (MIP_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lens fiber major intrinsic protein

Alternative name(s):
Aquaporin-0

Gene names

Name:	MIP
Synonyms:	AQP0

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

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 By similarity.
Subunit structure	Homotetramer. Homooctamer formed by head-to-head interaction between homotetramers from adjoining membranes By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein Probable. Cell junction › gap junction By similarity.
Tissue specificity	Detected in eye lens (at protein level). Ref.1
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 By similarity.
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	Sensory transduction Transport
Cellular component	Cell junction Cell membrane Gap junction Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Eye lens protein
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW
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_0000063911
Regions
	Topological domain	1 – 8	8	Cytoplasmic By similarity
	Transmembrane	9 – 32	24	Helical; By similarity
	Topological domain	33 – 38	6	Extracellular By similarity
	Transmembrane	39 – 61	23	Helical; By similarity
	Intramembrane	62 – 67	6	By similarity
	Intramembrane	68 – 78	11	Helical; By similarity
	Topological domain	79 – 84	6	Cytoplasmic By similarity
	Transmembrane	85 – 107	23	Helical; By similarity
	Topological domain	108 – 126	19	Extracellular By similarity
	Transmembrane	127 – 147	21	Helical; By similarity
	Topological domain	148 – 159	12	Cytoplasmic By similarity
	Transmembrane	160 – 176	17	Helical; By similarity
	Intramembrane	177 – 183	7	By similarity
	Intramembrane	184 – 194	11	Helical; By similarity
	Topological domain	195 – 200	6	Extracellular By similarity
	Transmembrane	201 – 219	19	Helical; By similarity
	Topological domain	220 – 263	44	Cytoplasmic By similarity
	Motif	68 – 70	3	NPA 1
	Motif	184 – 186	3	NPA 2
Amino acid modifications
	Modified residue	235	1	Phosphoserine Ref.1
	Modified residue	245	1	Deamidated asparagine; by deterioration Ref.1
	Modified residue	246	1	Deamidated asparagine; by deterioration Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6RZ07 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: DCC8D03F80E67E9B	FASTA	263	28,369
	10 20 30 40 50 60 MWELRSASFW RAIFAEFFAT LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALAXLVQTVG 70 80 90 100 110 120 HISGAHVNPA VTFXFLVGSQ MSLLRAFCYM AAQLLGAVAG AAVLYSVTPP AVRGNLALNT 130 140 150 160 170 180 LHAGVSVXQA TTVEIFLTLQ FVLCIFATYD ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG 190 200 210 220 230 240 AGMNPARSFA PAILTRNFTN HWVYWVGPII GGGLGSLLYD FLLFPRLKSV SERLSILKGT 250 260 RPSDNNGQPE GTGEPVELKT QAL

References

[1]

"Sequence and peptide map of guinea pig aquaporin 0." Han J., Little M., David L.L., Giblin F.J., Schey K.L. Mol. Vis. 10:215-222(2004) [PubMed: 15064681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, PHOSPHORYLATION AT SER-235, TISSUE SPECIFICITY, DEAMIDATION AT ASN-245 AND ASN-246.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY485151 mRNA. Translation: AAR37021.1.
3D structure databases
ProteinModelPortal	Q6RZ07.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000002379; ENSCPOP00000002132; ENSCPOG00000002347.
Phylogenomic databases
GeneTree	ENSGT00550000074347.
HOVERGEN	HBG000312.
InParanoid	Q6RZ07.
OrthoDB	EOG4CJVHW.
Family and domain databases
InterPro	IPR012269. Aquaporin. IPR023271. Aquaporin-like. IPR000425. MIP. [Graphical view]
Gene3D	G3DSA:1.20.1080.10. MIP. 1 hit.
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_CAVPO

Accession

Primary (citable) accession number: Q6RZ07

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2004
Last modified:	October 19, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program