Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26)

 MIP_BOVIN               Reviewed;         263 AA.
P06624;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 148.
RecName: Full=Lens fiber major intrinsic protein;
AltName: Full=Aquaporin-0;
AltName: Full=MIP26;
Short=MP26;
Name=MIP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-39.
PubMed=6207938; DOI=10.1016/0092-8674(84)90190-9;
Gorin M.B., Yancey S.B., Cline J., Revel J.-P., Horwitz J.;
"The major intrinsic protein (MIP) of the bovine lens fiber membrane:
characterization and structure based on cDNA cloning.";
Cell 39:49-59(1984).
[2]
PROTEIN SEQUENCE OF 1-33.
TISSUE=Lens;
PubMed=3882455; DOI=10.1016/0014-5793(85)81116-9;
Ngoc L.D., Paroutaud P., Dunia I., Benedetti E.L., Hoebeke J.;
"Sequence analysis of peptide fragments from the intrinsic membrane
protein of calf lens fibers MP26 and its natural maturation product
MP22.";
FEBS Lett. 181:74-78(1985).
[3]
PROTEIN SEQUENCE OF 239-259, PHOSPHORYLATION AT SER-243 AND SER-245,
AND DEAMIDATION AT ASN-246.
TISSUE=Lens;
PubMed=2176601; DOI=10.1111/j.1432-1033.1990.tb15650.x;
Lampe P.D., Johnson R.G.;
"Amino acid sequence of in vivo phosphorylation sites in the main
intrinsic protein (MIP) of lens membranes.";
Eur. J. Biochem. 194:541-547(1990).
[4]
PHOSPHORYLATION AT SER-235.
TISSUE=Lens;
PubMed=9375569;
Schey K.L., Fowler J.G., Schwartz J.C., Busman M., Dillon J.,
Crouch R.K.;
"Complete map and identification of the phosphorylation site of bovine
lens major intrinsic protein.";
Invest. Ophthalmol. Vis. Sci. 38:2508-2515(1997).
[5]
FUNCTION, INTERACTION WITH CALM, AND MUTAGENESIS OF TYR-149; LEU-227
AND VAL-230.
PubMed=23893133; DOI=10.1038/nsmb.2630;
Reichow S.L., Clemens D.M., Freites J.A., Nemeth-Cahalan K.L.,
Heyden M., Tobias D.J., Hall J.E., Gonen T.;
"Allosteric mechanism of water-channel gating by Ca(2+)-calmodulin.";
Nat. Struct. Mol. Biol. 20:1085-1092(2013).
[6]
FATTY ACYLATION.
PubMed=27378310; DOI=10.1016/j.bbamem.2016.06.026;
Ismail V.S., Mosely J.A., Tapodi A., Quinlan R.A., Sanderson J.M.;
"The lipidation profile of aquaporin-0 correlates with the acyl
composition of phosphoethanolamine lipids in lens membranes.";
Biochim. Biophys. Acta 1858:2763-2768(2016).
[7]
X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS), MEMBRANE TOPOLOGY, AND
SUBUNIT.
PubMed=15377788; DOI=10.1073/pnas.0405274101;
Harries W.E., Akhavan D., Miercke L.J., Khademi S., Stroud R.M.;
"The channel architecture of aquaporin 0 at a 2.2-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 101:14045-14050(2004).
[8]
X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS), MEMBRANE TOPOLOGY, AND
SUBUNIT.
PubMed=16309700; DOI=10.1016/j.jmb.2005.10.032;
Palanivelu D.V., Kozono D.E., Engel A., Suda K., Lustig A., Agre P.,
Schirmer T.;
"Co-axial association of recombinant eye lens aquaporin-0 observed in
loosely packed 3D crystals.";
J. Mol. Biol. 355:605-611(2006).
-!- FUNCTION: Water channel (PubMed:23893133). Channel activity is
down-regulated by CALM when cytoplasmic Ca(2+) levels are
increased. 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).
{ECO:0000250|UniProtKB:Q6J8I9, ECO:0000269|PubMed:23893133}.
-!- SUBUNIT: Homotetramer (PubMed:15377788, PubMed:16309700).
Homooctamer formed by head-to-head interaction between
homotetramers from adjoining membranes (PubMed:15377788,
PubMed:16309700). Interacts with CALM; one CALM molecule interacts
with the cytoplasmic domains of two aquaporins, leading to channel
closure (PubMed:23893133). {ECO:0000269|PubMed:15377788,
ECO:0000269|PubMed:16309700, ECO:0000269|PubMed:23893133}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q6J8I9}. Cell junction, gap junction
{ECO:0000250|UniProtKB:P30301}.
-!- 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.
-!- PTM: Subject to partial proteolytic cleavage in the eye lens core.
Partial proteolysis promotes interactions between tetramers from
adjoining membranes (By similarity). {ECO:0000250}.
-!- PTM: Fatty acylated at Met-1 and Lys-238. The acyl modifications,
in decreasing order of ion abundance, are: oleoyl (C18:1) >
palmitoyl (C16:0) > stearoyl (C18:0) > eicosenoyl (C20:1) >
dihomo-gamma-linolenoyl (C20:3) > palmitoleoyl (C16:1) >
eicosadienoyl (C20:2). {ECO:0000269|PubMed:27378310}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K02818; AAA30622.1; -; mRNA.
PIR; A23251; MMBOLM.
RefSeq; NP_776362.1; NM_173937.2.
UniGene; Bt.4516; -.
PDB; 1YMG; X-ray; 2.24 A; A=1-263.
PDB; 2C32; X-ray; 7.01 A; A=1-263.
PDBsum; 1YMG; -.
PDBsum; 2C32; -.
ProteinModelPortal; P06624; -.
SMR; P06624; -.
DIP; DIP-60546N; -.
IntAct; P06624; 1.
STRING; 9913.ENSBTAP00000013360; -.
TCDB; 1.A.8.8.2; the major intrinsic protein (mip) family.
iPTMnet; P06624; -.
PaxDb; P06624; -.
Ensembl; ENSBTAT00000013360; ENSBTAP00000013360; ENSBTAG00000010127.
GeneID; 280859; -.
KEGG; bta:280859; -.
CTD; 4284; -.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
GeneTree; ENSGT00760000119223; -.
HOGENOM; HOG000288286; -.
HOVERGEN; HBG000312; -.
InParanoid; P06624; -.
KO; K09863; -.
OMA; HLMGMYY; -.
OrthoDB; EOG091G166T; -.
TreeFam; TF312940; -.
Reactome; R-BTA-432047; Passive transport by Aquaporins.
EvolutionaryTrace; P06624; -.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000010127; -.
GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IMP:UniProtKB.
GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
GO; GO:0015250; F:water channel activity; IMP:UniProtKB.
GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
GO; GO:0006833; P:water transport; IMP:UniProtKB.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Complete proteome;
Direct protein sequencing; Eye lens protein; Gap junction;
Lipoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 263 Lens fiber major intrinsic protein.
/FTId=PRO_0000063910.
TOPO_DOM 1 8 Cytoplasmic.
TRANSMEM 9 32 Helical.
TOPO_DOM 33 38 Extracellular.
TRANSMEM 39 61 Helical.
INTRAMEM 62 67
INTRAMEM 68 78 Helical.
TOPO_DOM 79 84 Cytoplasmic.
TRANSMEM 85 107 Helical.
TOPO_DOM 108 126 Extracellular.
TRANSMEM 127 147 Helical.
TOPO_DOM 148 159 Cytoplasmic.
TRANSMEM 160 176 Helical.
INTRAMEM 177 183
INTRAMEM 184 194 Helical.
TOPO_DOM 195 200 Extracellular.
TRANSMEM 201 219 Helical.
TOPO_DOM 220 263 Cytoplasmic.
REGION 227 237 Interaction with CALM.
{ECO:0000269|PubMed:23893133}.
MOTIF 68 70 NPA 1.
MOTIF 184 186 NPA 2.
SITE 149 149 Important for water channel gating.
MOD_RES 235 235 Phosphoserine.
{ECO:0000269|PubMed:9375569}.
MOD_RES 243 243 Phosphoserine; by PKA.
{ECO:0000269|PubMed:2176601}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000269|PubMed:2176601}.
MOD_RES 246 246 Deamidated asparagine.
{ECO:0000269|PubMed:2176601}.
MUTAGEN 149 149 Y->G: Increases constitutive water
permeability. Abolishes regulation by
cytoplasmic calcium levels.
{ECO:0000269|PubMed:23893133}.
MUTAGEN 149 149 Y->L: Strongly decreases water
permeability. Abolishes regulation by
cytoplasmic calcium levels.
{ECO:0000269|PubMed:23893133}.
MUTAGEN 149 149 Y->S: Slightly decreases water
permeability, but has a minor effect on
the regulation by cytoplasmic calcium
levels. {ECO:0000269|PubMed:23893133}.
MUTAGEN 227 227 L->A: Strongly reduced CALM binding.
{ECO:0000269|PubMed:23893133}.
MUTAGEN 230 230 V->A: Strongly reduced CALM binding.
{ECO:0000269|PubMed:23893133}.
CONFLICT 14 14 C -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 29 33 GASLR -> RAFLL (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 10 31 {ECO:0000244|PDB:1YMG}.
HELIX 38 59 {ECO:0000244|PDB:1YMG}.
TURN 60 63 {ECO:0000244|PDB:1YMG}.
HELIX 69 77 {ECO:0000244|PDB:1YMG}.
HELIX 83 107 {ECO:0000244|PDB:1YMG}.
TURN 110 112 {ECO:0000244|PDB:1YMG}.
TURN 114 117 {ECO:0000244|PDB:1YMG}.
HELIX 127 149 {ECO:0000244|PDB:1YMG}.
HELIX 160 179 {ECO:0000244|PDB:1YMG}.
HELIX 185 195 {ECO:0000244|PDB:1YMG}.
TURN 199 202 {ECO:0000244|PDB:1YMG}.
HELIX 203 220 {ECO:0000244|PDB:1YMG}.
TURN 221 223 {ECO:0000244|PDB:1YMG}.
HELIX 230 238 {ECO:0000244|PDB:1YMG}.
SEQUENCE 263 AA; 28223 MW; E08C2C4F33398D4E CRC64;
MWELRSASFW RAICAEFFAS LFYVFFGLGA SLRWAPGPLH VLQVALAFGL ALATLVQAVG
HISGAHVNPA VTFAFLVGSQ MSLLRAICYM VAQLLGAVAG AAVLYSVTPP AVRGNLALNT
LHPGVSVGQA TIVEIFLTLQ FVLCIFATYD ERRNGRLGSV ALAVGFSLTL GHLFGMYYTG
AGMNPARSFA PAILTRNFTN HWVYWVGPVI GAGLGSLLYD FLLFPRLKSV SERLSILKGS
RPSESNGQPE VTGEPVELKT QAL


Related products :

Catalog number Product name Quantity
EIAAB24802 Aquaporin-0,Bos taurus,Bovine,Lens fiber major intrinsic protein,MIP,MIP26,MP26
EIAAB24798 Aquaporin-0,Lens fiber major intrinsic protein,Mip,MIP26,MP26,Rat,Rattus norvegicus
EIAAB24800 Aquaporin-0,Lens fiber major intrinsic protein,Mip,MIP26,Mouse,MP26,Mus musculus,Palm
EIAAB24801 AQP0,Aquaporin-0,Homo sapiens,Human,Lens fiber major intrinsic protein,MIP,MIP26,MP26
EIAAB24803 AQP0,Aquaporin-0,Chicken,Gallus gallus,Lens fiber major intrinsic protein,MIP,MIP26,MP26
EIAAB24799 Aquaporin-0,Lens fiber major intrinsic protein,MIP,Oryctolagus cuniculus,Rabbit
EIAAB24797 AQP0,Aquaporin-0,Canis familiaris,Canis lupus familiaris,Dog,Lens fiber major intrinsic protein,MIP
MIP_RAT Rat ELISA Kit FOR Lens fiber major intrinsic protein 96T
MIP_CANFA Dog ELISA Kit FOR Lens fiber major intrinsic protein 96T
MIPOL1 MIP Gene major intrinsic protein of lens fiber
CSB-EL013834DO Dog Lens fiber major intrinsic protein(MIP) ELISA kit 96T
CSB-EL013834CH Chicken Lens fiber major intrinsic protein(MIP) ELISA kit 96T
MIP_HUMAN Human ELISA Kit FOR Lens fiber major intrinsic protein 96T
CSB-EL013834BO Bovine Lens fiber major intrinsic protein(MIP) ELISA kit 96T
CSB-EL013834GU Guinea pig Lens fiber major intrinsic protein(MIP) ELISA kit 96T
E1382045 Monkey Major Intrinsic Protein of Lens Fiber (MIP) ELISA Kit
MIP_RABIT Rabbit ELISA Kit FOR Lens fiber major intrinsic protein 96T
E0762h Chicken ELISA Kit FOR Lens fiber major intrinsic protein 96T
SPT16_MOUSE Chicken ELISA Kit FOR Lens fiber major intrinsic protein 96T
CSB-EL013834DO Dog Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesDog 96T
CSB-EL013834CH Chicken Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesChicken 96T
CSB-EL013834RB Rabbit Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesRabbit 96T
CSB-EL013834GU Guinea pig Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesGuinea pig 96T
CSB-EL013834BO Bovine Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesBovine 96T
CSB-EL013834SH Sheep Lens fiber major intrinsic protein(MIP) ELISA kit SpeciesSheep 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur