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

Probable phospholipid-transporting ATPase IF (EC 3.6.3.1) (ATPase IR) (ATPase class VI type 11B) (P4-ATPase flippase complex alpha subunit ATP11B) (RING finger-binding protein) (Fragment)

 AT11B_RABIT             Reviewed;        1169 AA.
Q9N0Z4; Q8WMR2;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
30-APR-2003, sequence version 2.
05-DEC-2018, entry version 112.
RecName: Full=Probable phospholipid-transporting ATPase IF;
EC=7.6.2.1;
AltName: Full=ATPase IR;
AltName: Full=ATPase class VI type 11B;
AltName: Full=P4-ATPase flippase complex alpha subunit ATP11B;
AltName: Full=RING finger-binding protein;
Flags: Fragment;
Name=ATP11B;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION
(ISOFORM 2).
TISSUE=Endometrium;
PubMed=11058586; DOI=10.1074/jbc.M004231200;
Mansharamani M., Hewetson A., Chilton B.S.;
"Cloning and characterization of an atypical type IV P-type ATPase
that binds to the RING motif of RUSH transcription factors.";
J. Biol. Chem. 276:3641-3649(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 97-437 (ISOFORM 1).
STRAIN=New Zealand white; TISSUE=Leukocyte;
PubMed=11790799; DOI=10.1074/jbc.M200240200;
Halleck M.S., Schlegel R.A., Williamson P.L.;
"Reanalysis of ATP11B, a Type IV P-type ATPase.";
J. Biol. Chem. 277:9736-9740(2002).
[3]
INTERACTION WITH HLTF, AND MUTAGENESIS OF ILE-799.
PubMed=18584949; DOI=10.1016/j.mce.2008.05.007;
Hewetson A., Wright-Pastusek A.E., Helmer R.A., Wesley K.A.,
Chilton B.S.;
"Conservation of inter-protein binding sites in RUSH and RFBP, an
ATP11B isoform.";
Mol. Cell. Endocrinol. 292:79-86(2008).
-!- FUNCTION: Catalytic component of a P4-ATPase flippase complex
which catalyzes the hydrolysis of ATP coupled to the transport of
aminophospholipids from the outer to the inner leaflet of various
membranes and ensures the maintenance of asymmetric distribution
of phospholipids. Phospholipid translocation seems also to be
implicated in vesicle formation and in uptake of lipid signaling
molecules (By similarity). Isoform 2/RFBP appears to play a role
in the subnuclear trafficking of transcription factors with RING
motifs. {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=a phospholipid derivative(in) + ATP + H2O = a
phospholipid derivative(out) + ADP + H(+) + phosphate;
Xref=Rhea:RHEA:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16247, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:456216; EC=7.6.2.1;
-!- SUBUNIT: Component of a P4-ATPase flippase complex which consists
of a catalytic alpha subunit and an accessory beta subunit
(Probable). Interacts with TMEM30A. Isoform 2 interacts with HLTF
(via the RING-finger). {ECO:0000269|PubMed:18584949, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Recycling endosome membrane
{ECO:0000250|UniProtKB:Q9Y2G3}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9Y2G3}. Early endosome
{ECO:0000250|UniProtKB:Q9Y2G3}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q9Y2G3}. Golgi apparatus, trans-Golgi
network {ECO:0000250|UniProtKB:Q9Y2G3}. Note=Exit from the
endoplasmic reticulum requires the presence of TMEM30A, but not
TMEM30B. In the presence of TMEM30A, mainly located in recycling
endosomes. {ECO:0000250|UniProtKB:Q9Y2G3}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus inner membrane
{ECO:0000269|PubMed:11058586}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9N0Z4-1; Sequence=Displayed;
Name=2; Synonyms=RFBP;
IsoId=Q9N0Z4-2; Sequence=VSP_007308;
Note=Is missing the sequence which constitutes transmembrane
helix 4 and thus has an altered transmembrane architecture
compared to isoform 1. The long domain (amino acids 352-868),
which is normally cytoplasmic, extends into the nucleoplasm.
This isoform is unique to rabbit.;
-!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IV subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF236061; AAF68024.1; -; mRNA.
EMBL; AY069938; AAL57758.1; -; mRNA.
UniGene; Ocu.2522; -.
ProteinModelPortal; Q9N0Z4; -.
STRING; 9986.ENSOCUP00000024785; -.
eggNOG; KOG0206; Eukaryota.
eggNOG; ENOG410XPYK; LUCA.
HOGENOM; HOG000202528; -.
HOVERGEN; HBG050601; -.
InParanoid; Q9N0Z4; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:InterPro.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR030362; ATP11B.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006539; P-type_ATPase_IV.
InterPro; IPR032631; P-type_ATPase_N.
InterPro; IPR001757; P_typ_ATPase.
InterPro; IPR032630; P_typ_ATPase_c.
PANTHER; PTHR24092; PTHR24092; 1.
PANTHER; PTHR24092:SF57; PTHR24092:SF57; 1.
Pfam; PF16212; PhoLip_ATPase_C; 1.
Pfam; PF16209; PhoLip_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 1.
TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Endoplasmic reticulum; Endosome; Golgi apparatus; Lipid transport;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Translocase; Transmembrane;
Transmembrane helix; Transport.
CHAIN <1 1169 Probable phospholipid-transporting ATPase
IF.
/FTId=PRO_0000046372.
TOPO_DOM <1 47 Cytoplasmic. {ECO:0000255}.
TRANSMEM 48 69 Helical. {ECO:0000255}.
TOPO_DOM 70 74 Extracellular. {ECO:0000255}.
TRANSMEM 75 96 Helical. {ECO:0000255}.
TOPO_DOM 97 281 Cytoplasmic. {ECO:0000255}.
TRANSMEM 282 303 Helical. {ECO:0000255}.
TOPO_DOM 304 333 Extracellular. {ECO:0000255}.
TRANSMEM 334 351 Helical. {ECO:0000255}.
TOPO_DOM 352 868 Cytoplasmic. {ECO:0000255}.
TRANSMEM 869 890 Helical. {ECO:0000255}.
TOPO_DOM 891 902 Extracellular. {ECO:0000255}.
TRANSMEM 903 922 Helical. {ECO:0000255}.
TOPO_DOM 923 952 Cytoplasmic. {ECO:0000255}.
TRANSMEM 953 974 Helical. {ECO:0000255}.
TOPO_DOM 975 989 Extracellular. {ECO:0000255}.
TRANSMEM 990 1012 Helical. {ECO:0000255}.
TOPO_DOM 1013 1017 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1018 1039 Helical. {ECO:0000255}.
TOPO_DOM 1040 1057 Extracellular. {ECO:0000255}.
TRANSMEM 1058 1082 Helical. {ECO:0000255}.
TOPO_DOM 1083 1169 Cytoplasmic. {ECO:0000255}.
REGION 794 802 Required for binding to the RING-finger
of HLTF.
ACT_SITE 399 399 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 813 813 Magnesium. {ECO:0000250}.
METAL 817 817 Magnesium. {ECO:0000250}.
MOD_RES 1146 1146 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2G3}.
VAR_SEQ 327 392 Missing (in isoform 2).
{ECO:0000303|PubMed:11058586}.
/FTId=VSP_007308.
MUTAGEN 799 799 I->D: Increased binding to the RING-
finger of HLTF.
{ECO:0000269|PubMed:18584949}.
CONFLICT 133 133 R -> RGMHL (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 217 217 I -> V (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 283 283 I -> T (in Ref. 1; AAF68024).
{ECO:0000305}.
CONFLICT 299 299 L -> S (in Ref. 2; AAL57758).
{ECO:0000305}.
NON_TER 1 1
SEQUENCE 1169 AA; 133449 MW; D9A4CAE466A6528E CRC64;
LGFDPPHQSD TRTIYIANRF PQNGLYTPQK FIDNRIISSK YTVWNFVPKN LFEQFRRVAN
FYFLIIFLVQ LMIDTPTSPI TSGLPLFFVI TVTAIKQGYE DWLRHNSDNE VNGAPVYVVR
SGGLVKTRSK NIRVGDIVRI AKDEIFPADL VLLSSDRLDG SCHVTTASLD GETNLKTHVA
VPETAVLQTV ANLDTLVAVI ECQQPEADLY RFMGRMIITQ QMEEIVRPLG PESLLLRGAR
LKNTKEIFGV AVYTGMETKM ALNYKSKSQK RSAVEKSMNT FLIIYLIILI SEAIISTILK
YTWQAEEKWD EPWYNQKTEH QRNSSKILRF ISDFLAFLVL YNFIIPISLY VTVEMQKFLG
SFFIGWDLDL YHEESDQKAQ VNTSDLNEEL GQVEYVFTDK TGTLTENEMQ FRECSIHGMK
YQEINGRLVP EGPTPDSSEG NLSYLSSLSH VNSLSHLTSS SSFRTSPEND TELIKEHDLF
FKAVSLCHTV QISSVQTDGI GDGPWQSSLA PSQLEYYASS PDEKALVEAA ARIGIVFVGN
TEETMEVKIL GKLERYKLLH VLEFDSDRRR MSVIVQAPSG ERFLFAKGAE SSILPKCIGG
EIEKTRIHVD EFALKGLRTL CVAYRQFTSK EYEVIDRRLF EARTALQQRE EKLADVFHYI
EKDLILLGAT AVEDRLQDKV RETIEALRMA GIKVWVLTGD KHETAVSVSL SCGHFHRTMN
ILELTNQKSD SECAEQLRQL ARRITEDHVI QHGLVVDGTS LSLALREHEK LFMEVCRNCS
AVLCCRMAPL QKAKVIRLIK ISPEKPITIG CWDGANDVSM IQEAHVGIGI MGKERRQAAR
NSDYAIARFK FLSKLLFVHG HFYYIRIATL VQYFFYKNVC FITPQFLYQF YCLFSQQTLY
DSVYLTLYNI CFTSLPILIY SLLEQHIDPH ILQNKPTLYR DISKNRLLSI KTFLYWTILG
FSRSFIFLFG SYFLIGKDAS LLGNGQMFGN WTFGTLVFTV MVITVTVKMA LETHFWTWIN
HLVTWGSIIF YFVFSLFYGG ILWPFLGSQN MYFVFIQLVS SGSAWFAIIL MVVTCLFLDV
MKKVFDRQLH PTSTEKAQLT ETNSSIKCVD SLCCFPEGET TCTSVRRMLE RVIGRCSPTH
ISRSWSASDP FYTNDRSILT LSTMDSSTC


Related products :

Catalog number Product name Quantity
EIAAB45909 ATP6V0A2,Homo sapiens,Human,Lysosomal H(+)-transporting ATPase V0 subunit a2,TJ6,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 k
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1
EIAAB45649 ATP6A1,ATP6V1A,ATP6V1A1,Homo sapiens,Human,Vacuolar ATPase isoform VA68,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,VPP2,V-type proton ATPase catalytic subunit A
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
G1342 Probable phospholipid-transporting ATPase IF (ATP11B), Rabbit, ELISA Kit 96T
G1341 Probable phospholipid-transporting ATPase IF (ATP11B), Human, ELISA Kit 96T
CSB-EL002314HU Human Probable phospholipid-transporting ATPase IF(ATP11B) ELISA kit 96T
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
EIAAB45631 Atp6ap1,Atp6ip1,Atp6s1,Mouse,Mus musculus,Protein C7-1,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
CSB-EL002314RB Rabbit Probable phospholipid-transporting ATPase IF(ATP11B) ELISA kit SpeciesRabbit 96T
CSB-EL002314HU Human Probable phospholipid-transporting ATPase IF(ATP11B) ELISA kit SpeciesHuman 96T
AT11B_HUMAN ELISA Kit FOR Probable phospholipid-transporting ATPase IF; organism: Human; gene name: ATP11B 96T
EIAAB45563 32 kDa accessory protein,ATP6D,ATP6V0D1,Homo sapiens,Human,p39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB45564 32 kDa accessory protein,ATP6D,ATP6V0D1,Bos taurus,Bovine,P39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB45652 Atp6a1,Atp6a2,Atp6v1a,Atp6v1a1,Mouse,Mus musculus,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45651 ATP6A1,ATP6V1A,ATP6V1A1,Bos taurus,Bovine,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB45650 ATP6A1,ATP6V1A,ATP6V1A1,Pig,Sus scrofa,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,V-type proton ATPase catalytic subunit A
EIAAB32660 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,Proteasome 26S subunit ATPase 4,Psmc4,Rat,Rattus norvegicus,S6 ATPase,Tat-binding protein 7,Tbp7,TBP-7
EIAAB45669 ATP6M,ATP6V1D,Oryctolagus cuniculus,Rabbit,Vacuolar proton pump subunit D,VATD,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB45668 ATP6M,ATP6V1D,Homo sapiens,Human,Vacuolar proton pump subunit D,VATD,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB41972 15S Mg(2+)-ATPase p97 subunit,Mouse,Mus musculus,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,Vcp


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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