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

Exportin-2 (Exp2) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter)

 XPO2_DANRE              Reviewed;         971 AA.
Q7SZC2; G1K2H9;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 2.
05-JUL-2017, entry version 86.
RecName: Full=Exportin-2;
Short=Exp2;
AltName: Full=Chromosome segregation 1-like protein;
AltName: Full=Importin-alpha re-exporter;
Name=cse1l; Synonyms=xpo2;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1] {ECO:0000312|Ensembl:ENSDARP00000022858, ECO:0000312|Proteomes:UP000000437}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen {ECO:0000312|Ensembl:ENSDARP00000022858,
ECO:0000312|Proteomes:UP000000437};
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=AB; TISSUE=Kidney;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, INTERACTION WITH CFTR, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=20933420; DOI=10.1016/j.cub.2010.09.012;
Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S.,
Gabriel S., Mostov K., Huisken J., Stainier D.Y.;
"Cse1l is a negative regulator of CFTR-dependent fluid secretion.";
Curr. Biol. 20:1840-1845(2010).
-!- FUNCTION: Export receptor for importin alpha. Mediates importin-
alpha re-export from the nucleus to the cytoplasm after import
substrates have been released into the nucleoplasm (By
similarity). Negatively regulates fluid secretion and plays a role
in fluid homeostasis by downregulating cftr activity
(PubMed:20933420). {ECO:0000250|UniProtKB:P55060,
ECO:0000269|PubMed:20933420}.
-!- SUBUNIT: Interacts with cftr (PubMed:20933420).
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20933420}.
Nucleus {ECO:0000250|UniProtKB:P55060}. Apical cell membrane
{ECO:0000269|PubMed:20933420}; Peripheral membrane protein
{ECO:0000305|PubMed:20933420}. Basal cell membrane
{ECO:0000269|PubMed:20933420}; Peripheral membrane protein
{ECO:0000305|PubMed:20933420}. Lateral cell membrane
{ECO:0000269|PubMed:20933420}; Peripheral membrane protein
{ECO:0000305|PubMed:20933420}. Note=Shuttles between the nucleus
and the cytoplasm. {ECO:0000250|UniProtKB:P55060}.
-!- TISSUE SPECIFICITY: Detected in larval gut, liver, exocrine
pancreas and part of the brain and retina at 96 hpf.
{ECO:0000269|PubMed:20933420}.
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
strong expansion of the gut lumen, due to excessive fluid
accumulation. {ECO:0000269|PubMed:20933420}.
-!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CR559931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052479; AAH52479.1; -; mRNA.
EMBL; BC066737; AAH66737.1; -; mRNA.
RefSeq; NP_958858.1; NM_201450.1.
UniGene; Dr.75377; -.
ProteinModelPortal; Q7SZC2; -.
BioGrid; 78862; 1.
STRING; 7955.ENSDARP00000022858; -.
PaxDb; Q7SZC2; -.
PRIDE; Q7SZC2; -.
Ensembl; ENSDART00000013203; ENSDARP00000022858; ENSDARG00000006963.
GeneID; 30707; -.
KEGG; dre:30707; -.
CTD; 1434; -.
ZFIN; ZDB-GENE-990603-1; cse1l.
eggNOG; KOG1992; Eukaryota.
eggNOG; COG5657; LUCA.
GeneTree; ENSGT00550000074884; -.
HOGENOM; HOG000201317; -.
HOVERGEN; HBG080050; -.
InParanoid; Q7SZC2; -.
KO; K18423; -.
OMA; FMPYVFQ; -.
OrthoDB; EOG091G01TH; -.
PhylomeDB; Q7SZC2; -.
TreeFam; TF300473; -.
PRO; PR:Q7SZC2; -.
Proteomes; UP000000437; Chromosome 11.
Bgee; ENSDARG00000006963; -.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
GO; GO:0005049; F:nuclear export signal receptor activity; IBA:GO_Central.
GO; GO:0008536; F:Ran GTPase binding; IEA:InterPro.
GO; GO:0007589; P:body fluid secretion; IMP:ZFIN.
GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR005043; CAS_CSE1_C.
InterPro; IPR013713; Cse1.
InterPro; IPR001494; Importin-beta_N.
Pfam; PF03378; CAS_CSE1; 1.
Pfam; PF08506; Cse1; 1.
Pfam; PF03810; IBN_N; 1.
SMART; SM00913; IBN_N; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50166; IMPORTIN_B_NT; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Membrane; Nucleus;
Protein transport; Reference proteome; Transport.
CHAIN 1 971 Exportin-2.
/FTId=PRO_0000237680.
DOMAIN 29 102 Importin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00115}.
CONFLICT 48 48 A -> T (in Ref. 2; AAH52479/AAH66737).
SEQUENCE 971 AA; 110028 MW; 632AFF088108925D CRC64;
MELNDGNLQT LTEYLQKTLS ADPAVRRPAE KFLESVEGNQ NYPILLLAVL EKSQNEVIRV
CSAVTFKNYI KRNWRIVEDE PNKISDPDRT AIKANIVNLM LTSPEQIQKQ LSDAISIIGR
EDFPLKWPDL LTEMVNRFQS GDFHIINGVL RTAHSLFKRY RHEFKSNELW SEIKLVLDTF
AQPLTELFKA TIELCQTHAT DINALKVLFS SLTLISKLFY SLNFQDLPEF FEDNMETWMT
NFHNLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQPYL PRFVTAIWNL
LVTTGQEVKY DLLVSNAIQF LASVCERPHY KHLFEDQNVL TSICEKVIVP NMEFRSADEE
AFEDNSEEYI IRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLAEYAKNP
GVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLSEF FLNHILIDLK SPNVNEFPVL
KSDAIKYVMT FRSQLPKEQL LQAVPLLVSH LQAESIVQHT YAAHALERLF TMRGGNNTTL
ITPTEMAPFT EQLLNHLFKA LAIPGSSENE YIMKAIMRSF SLLQEAIVPY IPTLIGQLTH
KLLLVSKNPS KPHFNHYLFE SLCLSIRITC KANPDTVSSF EEALFPVFTE ILQNDVQEFV
PYVFQVMSLL LEIHSNSIPS SYMALFPHLL QPVLWERTGN IPPLVRLLQA YLEKGAAAIA
NTASDKIPGL LGVFQKLIAS KANDHQGFYL LNSIVEHMPA EAITQYRKQI FILLFQRLQS
SKTTKFVKSF LVFINLYSVK YGAIALQEIF DDIQPKMFGM VVEKIVIPEV QKVSGQVEKK
ICAVGIIKIL TECPAMMDTE YTKLWAPLLQ ALIGLFELPE DDSIPDDEHF IDIEDTPGYQ
TAFSQLAFAG KKEHDPIGDA VSNPKILLAQ SLHKLSTACP GRVPSMLSTS LPTEALQFLQ
GYLQAATVQL V


Related products :

Catalog number Product name Quantity
EIAAB46549 Chromosome segregation 1-like protein,Cse1l,Exp2,Exportin-2,Importin-alpha re-exporter,Mouse,Mus musculus,Xpo2
EIAAB46548 Bos taurus,Bovine,Chromosome segregation 1-like protein,CSE1L,Exp2,Exportin-2,Importin-alpha re-exporter,XPO2
EIAAB46547 CAS,Cellular apoptosis susceptibility protein,Chromosome segregation 1-like protein,CSE1L,Exp2,Exportin-2,Homo sapiens,Human,Importin-alpha re-exporter,XPO2
EIAAB38755 Chromosome segregation protein SmcB,Mouse,Mus musculus,Sb1.8,Sb1.8,SMC protein 1A,Smc1,Smc1a,SMC-1A,SMC-1-alpha,Smc1l1,Smcb,Structural maintenance of chromosomes protein 1A
26-946 Meiotic recombination and chromosome segregation require the formation of double-strand breaks (DSBs) in paired chromosome homologs. During meiosis in yeast, a meiotic recombination protein is covalen 0.05 mg
EIAAB31632 Homo sapiens,Human,PMS2L5,PMS2P5,PMS4,PMS7,Postmeiotic segregation increased 2-like protein 5,Postmeiotic segregation increased protein 4,Postmeiotic segregation increased protein 7,Putative postmeiot
27-036 Condensin complexes I and II play essential roles in mitotic chromosome assembly and segregation. Both condensins contain 2 invariant structural maintenance of chromosome (SMC) subunits, SMC2 and SMC4 0.05 mg
27-035 Condensin complexes I and II play essential roles in mitotic chromosome assembly and segregation. Both condensins contain 2 invariant structural maintenance of chromosome (SMC) subunits, SMC2 and SMC4 0.05 mg
EIAAB31630 Homo sapiens,Human,PMS2L14,PMS2L2,PMS2P2,PMS4,Postmeiotic segregation increased 2-like protein 14,Postmeiotic segregation increased protein 4,Putative postmeiotic segregation increased 2 pseudogene 2,
EIAAB31629 Homo sapiens,hPMS3,Human,PMS2L1,PMS2L13,PMS2L6,PMS2L8,PMS2P1,PMS2-related protein 2,PMS3,PMS8,PMSR2,Postmeiotic segregation increased 2-like protein 13,Postmeiotic segregation increased 2-like protein
CSF1R CSE1L Gene CSE1 chromosome segregation 1-like (yeast)
EIAAB38766 Bam,Bamacan,Basement membrane-associated chondroitin proteoglycan,Bmh,Chondroitin sulfate proteoglycan 6,Chromosome segregation protein SmcD,Cspg6,Rat,Rattus norvegicus,SMC protein 3,Smc3,SMC-3,Smc3l1
EIAAB31631 Homo sapiens,Human,PMS2L3,PMS2L9,PMS2P3,PMS2-related protein 3,PMS5,PMSR3,Postmeiotic segregation increased 2-like protein 9,Postmeiotic segregation increased protein 5,Putative postmeiotic segregatio
EIAAB38763 Bam,Bamacan,Basement membrane-associated chondroitin proteoglycan,Bmh,Chondroitin sulfate proteoglycan 6,Chromosome segregation protein SmcD,Cspg6,Mad member-interacting protein 1,Mmip1,Mouse,Mus musc
EIAAB46545 Chromosome region maintenance 1 protein homolog,Crm1,Exp1,Exportin-1,Rat,Rattus norvegicus,Xpo1
EIAAB46544 Chromosome region maintenance 1 protein homolog,Crm1,Exp1,Exportin-1,Mouse,Mus musculus,Xpo1
EIAAB46546 Chromosome region maintenance 1 protein homolog,CRM1,Exp1,Exportin-1,Homo sapiens,Human,XPO1
EIAAB31633 Homo sapiens,Human,PMS2L11,PMS2P11,PMS2-related protein 6,PMSR6,Putative postmeiotic segregation increased 2 pseudogene 11,Putative postmeiotic segregation increased 2-like protein 11
GWB-F0D64F Chromosome Segregation Gene Homolog Cas (CSE1L) Rabbit anti-Human Polyclonal (N-Terminus) Antibody
27-790 PMF1 is part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. It may act as a cotranscription partner of NFE2L2 involved 0.05 mg
27-365 PMF1 is part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. It may act as a cotranscription partner of NFE2L2 involved 0.1 mg
28-971 PMF1 is part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. It may act as a cotranscription partner of NFE2L2 involved 0.05 mg
CSB-EL006042HU Human CSE1 chromosome segregation 1-like (yeast) (CSE1L) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006042MO Mouse CSE1 chromosome segregation 1-like (yeast) (CSE1L) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL006042BO Bovine CSE1 chromosome segregation 1-like (yeast) (CSE1L) ELISA kit, Species Bovine, Sample Type serum, plasma 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