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Ras-related protein Rab-10 (Rab-10)

 RAB10_CAEEL             Reviewed;         201 AA.
Q94148; I7FXD6;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
23-MAY-2018, entry version 140.
RecName: Full=Ras-related protein Rab-10 {ECO:0000305};
Short=Rab-10 {ECO:0000303|PubMed:16394106};
Name=rab-10 {ECO:0000303|PubMed:16394106, ECO:0000312|EMBL:CCD70773.1,
ECO:0000312|WormBase:T23H2.5};
ORFNames=T23H2.5 {ECO:0000312|WormBase:T23H2.5};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|EMBL:CCD70773.1};
[1] {ECO:0000312|EMBL:CCD70773.1, ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD70773.1,
ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000312|EMBL:AFP33152.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 2-201, MUTAGENESIS OF THR-23 AND GLN-68,
AND PHYLOGENETIC ANALYSIS.
PubMed=23185324; DOI=10.1371/journal.pone.0049387;
Gallegos M.E., Balakrishnan S., Chandramouli P., Arora S.,
Azameera A., Babushekar A., Bargoma E., Bokhari A., Chava S.K.,
Das P., Desai M., Decena D., Saramma S.D., Dey B., Doss A.L., Gor N.,
Gudiputi L., Guo C., Hande S., Jensen M., Jones S., Jones N.,
Jorgens D., Karamchedu P., Kamrani K., Kolora L.D., Kristensen L.,
Kwan K., Lau H., Maharaj P., Mander N., Mangipudi K., Menakuru H.,
Mody V., Mohanty S., Mukkamala S., Mundra S.A., Nagaraju S.,
Narayanaswamy R., Ndungu-Case C., Noorbakhsh M., Patel J., Patel P.,
Pendem S.V., Ponakala A., Rath M., Robles M.C., Rokkam D., Roth C.,
Sasidharan P., Shah S., Tandon S., Suprai J., Truong T.Q.,
Uthayaruban R., Varma A., Ved U., Wang Z., Yu Z.;
"The C. elegans Rab family: Identification, classification and toolkit
construction.";
PLoS ONE 7:E49387-E49387(2012).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF THR-23 AND GLN-68.
PubMed=16394106; DOI=10.1091/mbc.E05-08-0787;
Chen C.C., Schweinsberg P.J., Vashist S., Mareiniss D.P., Lambie E.J.,
Grant B.D.;
"RAB-10 is required for endocytic recycling in the Caenorhabditis
elegans intestine.";
Mol. Biol. Cell 17:1286-1297(2006).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=17761527; DOI=10.1091/mbc.E07-05-0486;
Glodowski D.R., Chen C.C., Schaefer H., Grant B.D., Rongo C.;
"RAB-10 regulates glutamate receptor recycling in a cholesterol-
dependent endocytosis pathway.";
Mol. Biol. Cell 18:4387-4396(2007).
[5]
INTERACTION WITH EHBP-1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF THR-23 AND GLN-68.
PubMed=20573983; DOI=10.1091/mbc.E10-02-0149;
Shi A., Chen C.C., Banerjee R., Glodowski D., Audhya A., Rongo C.,
Grant B.D.;
"EHBP-1 functions with RAB-10 during endocytic recycling in
Caenorhabditis elegans.";
Mol. Biol. Cell 21:2930-2943(2010).
[6]
FUNCTION, ENZYME REGULATION, INTERACTION WITH TBC-2, SUBCELLULAR
LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-23 AND GLN-68.
PubMed=23100538; DOI=10.1073/pnas.1203306109;
Sasidharan N., Sumakovic M., Hannemann M., Hegermann J., Liewald J.F.,
Olendrowitz C., Koenig S., Grant B.D., Rizzoli S.O., Gottschalk A.,
Eimer S.;
"RAB-5 and RAB-10 cooperate to regulate neuropeptide release in
Caenorhabditis elegans.";
Proc. Natl. Acad. Sci. U.S.A. 109:18944-18949(2012).
[7]
FUNCTION, INTERACTION WITH CNT-1 AND EHBP-1, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=22869721; DOI=10.1073/pnas.1205278109;
Shi A., Liu O., Koenig S., Banerjee R., Chen C.C., Eimer S.,
Grant B.D.;
"RAB-10-GTPase-mediated regulation of endosomal phosphatidylinositol-
4,5-bisphosphate.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2306-E2315(2012).
[8]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF THR-23 AND GLN-68.
PubMed=25301900; DOI=10.1073/pnas.1408327111;
Chen S., Li L., Li J., Liu B., Zhu X., Zheng L., Zhang R., Xu T.;
"SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-
independent cargo through endosomal tubules in Caenorhabditis
elegans.";
Proc. Natl. Acad. Sci. U.S.A. 111:15432-15437(2014).
[9]
FUNCTION, INTERACTION WITH AMPH-1 AND TBC-2, SUBCELLULAR LOCATION,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLN-68.
PubMed=26393361; DOI=10.1371/journal.pgen.1005514;
Liu O., Grant B.D.;
"Basolateral endocytic recycling requires RAB-10 and AMPH-1 mediated
recruitment of RAB-5 GAP TBC-2 to endosomes.";
PLoS Genet. 11:E1005514-E1005514(2015).
[10]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF THR-23 AND GLN-68.
PubMed=26394140; DOI=10.1371/journal.pgen.1005484;
Zou W., Yadav S., DeVault L., Nung Jan Y., Sherwood D.R.;
"RAB-10-dependent membrane transport is required for dendrite
arborization.";
PLoS Genet. 11:E1005484-E1005484(2015).
[11]
FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
THR-23 AND GLN-68.
PubMed=26633194; DOI=10.1371/journal.pgen.1005695;
Taylor C.A., Yan J., Howell A.S., Dong X., Shen K.;
"RAB-10 regulates dendritic branching by balancing dendritic
transport.";
PLoS Genet. 11:E1005695-E1005695(2015).
-!- FUNCTION: The small GTPases Rab are key regulators of
intracellular membrane trafficking, from the formation of
transport vesicles to their fusion with membranes. Rabs cycle
between an inactive GDP-bound form and an active GTP-bound form
that is able to recruit to membranes different set of downstream
effectors directly responsible for vesicle formation, movement,
tethering and fusion (PubMed:23100538, PubMed:26394140,
PubMed:26633194). Required for basolateral endocytic recycling,
the return of macromolecules and fluid from endosomes to the
plasma membrane, in polarized epithelial cells of the intestine
upstream of rme-1 (PubMed:16394106). Involved in the formation of
the endosomal tubular network that is required for basolateral
recycling of clathrin-independent endocytic cargo such as daf-4 in
the intestine (PubMed:25301900). Required for the recruitment of
cnt-1 effector to endosomal membranes in the intestinal
epithelium, which is important for the regulation of levels of
endosomal phosphatidylinositol-4,5-bisphosphate, a key
phosphoinositide in membrane traffic, and for the recruitment of
endosomal membrane-bending proteins, rme-1 and sdpn-1
(PubMed:22869721). Recruits the rab-5 GTPase-activating protein
tbc-2 to endosomes where it then inactivates rab-5 resulting in
removal of rab-5 from membranes, which is necessary for cargo
transport from early endosomes to recycling endosomes in the
basolateral intestine (PubMed:26393361). Regulates recycling of
synaptic membrane AMPA glutamate receptor, glr-1, from
intracellular endosomal compartments back to synapses in a
cholesterol-dependent endocytosis pathway functioning after
clathrin-independent endocytosis in command interneurons
(PubMed:17761527). Regulates neuropeptide release from dense core
vesicles (DCVs) of cholinergic motoneurons in cooperation with
rab-5. They reciprocally recruite each other's inactivating GAP
molecule leading to local exclusion of one or the other rab
protein at the Golgi-endosomal interphase at an essential stage
during DCV sorting (PubMed:23100538). Regulates membrane
trafficking of membranes and dendrite proteins from the Golgi
and/or endosomal compartments to plasma membrane during dendrite
morphogenesis together with the exocyst complex in the multi-
dendritic PVD sensory neurons acting in a cell-autonomous manner
and requiring its GTPase activity (PubMed:26394140). Functions
cell-autonomously together with the exocyst complex to regulate
dendrite morphogenesis and anterior-posterior patterning of the
PVD neurons dendritic arbor by balancing the anterograde and
retrograde transport via molecular motors unc-116 (kinesin heavy
chain) and dhc-1 (dynein heavy chain) to appropriately transport
branching factors, such as dma-1, to the specific subcellular
regions of the developing dendrite in its GTPase activity-
dependent manner (PubMed:26633194). {ECO:0000269|PubMed:16394106,
ECO:0000269|PubMed:17761527, ECO:0000269|PubMed:22869721,
ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:25301900,
ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140,
ECO:0000269|PubMed:26633194}.
-!- ENZYME REGULATION: Rab activation is generally mediated by a
guanine exchange factor (GEF), while inactivation through
hydrolysis of bound GTP is catalyzed by a GTPase activating
protein (GAP) (By similarity). Tbc-4 is a likely GAP of this rab
(PubMed:23100538). Denn-4 is a putative GEF of this rab
(PubMed:26633194). {ECO:0000250|UniProtKB:Q15286,
ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:26633194}.
-!- SUBUNIT: Interacts (GTP-bound form) with ehbp-1 (via C-terminal
coiled coil) (PubMed:20573983, PubMed:22869721). Interacts (GTP-
bound form) with cnt-1 (via C-terminal ankyrin repeat)
(PubMed:22869721). Interacts (GTP-bound form) with rab-5 GAP, tbc-
2 (via putative coiled coil domain) (PubMed:23100538,
PubMed:26393361). Interacts (GTP-bound form) with amph-1
(PubMed:26393361). {ECO:0000269|PubMed:20573983,
ECO:0000269|PubMed:22869721, ECO:0000269|PubMed:23100538,
ECO:0000269|PubMed:26393361}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:26394140}; Lipid-
anchor {ECO:0000250|UniProtKB:P62491}. Late endosome membrane
{ECO:0000269|PubMed:16394106}; Lipid-anchor
{ECO:0000250|UniProtKB:P62491}. Golgi apparatus membrane
{ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:26394140}; Lipid-
anchor {ECO:0000250|UniProtKB:P62491}. Endosome membrane
{ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:26393361}; Lipid-
anchor {ECO:0000250|UniProtKB:P62491}. Note=Colocalizes with cnt-1
on recycling endosomes in the intestinal epithelium in vivo
(PubMed:22869721). Colocalizes with cnt-1, tbc-2 and amph-1 on
endosomes in the intestinal epithelium (PubMed:26393361).
Localizes at tips of the growing basolateral endosomal tubules of
the intestine (PubMed:25301900). Present in cell bodies as well as
throughout the ventral nerve cord of sensory interneurons
(PubMed:17761527). The localization on endosomal structures of the
intestine and interneurons is regulated by ehbp-1
(PubMed:20573983). Localizes to the medial Golgi, endosomes and
immature dense core vesicles (DCVs) in ventral nerve cord (VNC)
neurons. Also enriched in axons at dorsal nerve cord (DNC)
synapses and localizes with synaptic vesicles and DCVs. Some
localize with DCV in neuronal cell bodies. Colocalizes with tbc-4
in the cell body near the Golgi in VNC neurons (PubMed:23100538).
Localizes to the Golgi and the early endosomes in the PVD sensory
neurons. Localizes to the transport vesicles moving bi-
directionally along PVD dendrites. Colocalizes with exoc-8 on
intracellular vesicles in the PVD dendrites (PubMed:26394140).
{ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:17761527,
ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:22869721,
ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:25301900,
ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140}.
-!- TISSUE SPECIFICITY: Almost ubiquitously expressed. Expressed in
intestine, hypodermis, seam cells, body-wall muscles, many
neurons, oviduct sheath cell, spermatheca, coelomocytes and
pharyngeal and nerve ring. {ECO:0000269|PubMed:16394106}.
-!- DISRUPTION PHENOTYPE: Intestinal cells exhibit abnormally abundant
rab-5 and rab-7 positive enlarged early endosomes, which
accumulate basolaterally recycling transmembrane cargo molecules
and fluid indicating a block in basolateral transport
(PubMed:16394106, PubMed:20573983). On the other hand, rme-1
positive recycling endosomes are missing. No endocytic trafficking
defects in oocytes or coelomocytes (PubMed:16394106). Almost
complete loss of cnt-1 endosomal localization in the intestinal
epithelium. Overaccumulation of endosomal phosphatidylinositol-
4,5-bisphosphate (PubMed:22869721). Nearly complete loss of
basolateral endosomal tubule extensions of the intestine
(PubMed:25301900). The endosomal localization of tbc-2 is strongly
reduced leading to increased rab-5 association with membranes in
the intestinal epithelia (PubMed:26393361). Cholesterol-dependent
accumulation of glr-1 in large accretions running along the length
of the ventral cord neurite bundle while synapses don't have
general formation defects. Animals display a decreased frequency
of locomotional reversals and significantly reduced response to
nose-touch suggesting reduced glr-1 signaling (PubMed:17761527,
PubMed:20573983). Rab-10 lin-10 double mutant displays additive
glr-1 trafficking defects indicating that they both regulate
endocytic recycling of AMPA receptors to synapses, but most
probably along distinct regulatory pathways (PubMed:17761527).
Complete loss of dense core vesicles (DCVs) secretion of
neuropeptides from DA/DB motoneurons, while synaptic
ultrastructure and synaptic vesicles (SV) exocytosis as well as
coelomocyte function are unaffected (PubMed:23100538). Severely
reduced proximal dendritic arborization in multi-dendritic PVD
sensory neurons, but minimal effect on dendritic branching and
growth on the distal area of the PVD. The growth of PVD axon is
normal. Reduced dendritic growth of the multi-dendritic FLP
neurons, but no effect on the dendritic growth of unbranched
dendrites of the OLL, AWB and AWC neurons. Accumulates dendritic
membrane proteins dma-1 and hpo-30 within intracellular vesicles
within the growing PVD dendrites and have decreased dendrite
membrane localization of these proteins. Rab-10 rab-8 double
deletion mutant has enhanced dendritic arborization defects than
rab-10 deletion alone in PVD neurons (PubMed:26394140). PVD
dendritic branches are reduced in the posterior region of the
cell, but are excessive in the distal anterior region of the cell.
Dma-1 fails to localize to the plasma membrane in the posterior
dendrite (PubMed:26633194). Rab-10 rab-8 double deletion mutant
has disrupted transport of membrane proteins to the plasma
membrane of the nonpolarized germline cells (PubMed:20573983).
{ECO:0000269|PubMed:16394106, ECO:0000269|PubMed:17761527,
ECO:0000269|PubMed:20573983, ECO:0000269|PubMed:22869721,
ECO:0000269|PubMed:23100538, ECO:0000269|PubMed:25301900,
ECO:0000269|PubMed:26393361, ECO:0000269|PubMed:26394140,
ECO:0000269|PubMed:26633194}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
{ECO:0000305}.
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EMBL; BX284601; CCD70773.1; -; Genomic_DNA.
EMBL; JQ235188; AFP33152.1; -; mRNA.
PIR; T28971; T28971.
RefSeq; NP_491857.1; NM_059456.4.
UniGene; Cel.17301; -.
ProteinModelPortal; Q94148; -.
SMR; Q94148; -.
IntAct; Q94148; 1.
STRING; 6239.T23H2.5.1; -.
EPD; Q94148; -.
PaxDb; Q94148; -.
EnsemblMetazoa; T23H2.5.1; T23H2.5.1; WBGene00004273.
EnsemblMetazoa; T23H2.5.2; T23H2.5.2; WBGene00004273.
GeneID; 266836; -.
KEGG; cel:CELE_T23H2.5; -.
UCSC; T23H2.5.1; c. elegans.
CTD; 266836; -.
WormBase; T23H2.5; CE14114; WBGene00004273; rab-10.
eggNOG; KOG0078; Eukaryota.
eggNOG; ENOG410XPUI; LUCA.
GeneTree; ENSGT00890000139330; -.
HOGENOM; HOG000233968; -.
InParanoid; Q94148; -.
KO; K07903; -.
OMA; NKCDWED; -.
OrthoDB; EOG091G0LA6; -.
PhylomeDB; Q94148; -.
Reactome; R-CEL-6798695; Neutrophil degranulation.
Reactome; R-CEL-8873719; RAB geranylgeranylation.
Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
PRO; PR:Q94148; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00004273; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0031045; C:dense core granule; IDA:WormBase.
GO; GO:0005769; C:early endosome; IDA:WormBase.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:WormBase.
GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
GO; GO:0005797; C:Golgi medial cisterna; IDA:WormBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0032593; C:insulin-responsive compartment; IBA:GO_Central.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0055037; C:recycling endosome; IDA:WormBase.
GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO; GO:0071532; F:ankyrin repeat binding; IMP:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0032794; F:GTPase activating protein binding; IPI:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
GO; GO:0032456; P:endocytic recycling; IMP:WormBase.
GO; GO:1902647; P:negative regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process; IMP:UniProtKB.
GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
GO; GO:0009306; P:protein secretion; IBA:GO_Central.
GO; GO:0001881; P:receptor recycling; IMP:WormBase.
GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
1: Evidence at protein level;
Complete proteome; Endosome; Golgi apparatus; GTP-binding;
Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
Protein transport; Reference proteome; Transport.
CHAIN 1 201 Ras-related protein Rab-10.
/FTId=PRO_0000438074.
NP_BIND 16 23 GTP. {ECO:0000250|UniProtKB:P07560}.
NP_BIND 64 68 GTP. {ECO:0000250|UniProtKB:P07560}.
NP_BIND 122 125 GTP. {ECO:0000250|UniProtKB:P62491}.
NP_BIND 152 154 GTP. {ECO:0000250|UniProtKB:P62491}.
MOTIF 38 46 Effector region. {ECO:0000305}.
LIPID 200 200 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P62491}.
LIPID 201 201 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P62491}.
MUTAGEN 23 23 T->N: Dominant-negative mutant.
Mislocalizes to the cytoplasm instead of
membranes. Hardly any basolateral
endosomal tubules of the intestine. No
interaction with catalytically inactive
tbc-4 A-155 mutant. Does not rescue rab-
10 null mutant, and fails to rescue the
proximal PVD defects in rab-10 deletion
mutants, but also disrupts the distal
dendrite arbor and further reduces branch
complexity in the anterior region in
wild-type animals.
{ECO:0000269|PubMed:16394106,
ECO:0000269|PubMed:20573983,
ECO:0000269|PubMed:23100538,
ECO:0000269|PubMed:23185324,
ECO:0000269|PubMed:25301900,
ECO:0000269|PubMed:26394140,
ECO:0000269|PubMed:26633194}.
MUTAGEN 68 68 Q->L: Constitutively active mutant unable
to hydrolyze GTP. Associates correctly
with membranes. Displays more extensive
network of basolateral endosomal tubules
of the intestine. Strongly reduced DCV
secretion in dorsally projecting
cholinergic DA/DB motoneurons. Interacts
with the catalytically inactive tbc-4 A-
155 mutant, but not with the
catalytically active tbc-4. Partially
rescues rab-10 null mutant and fully
rescues the PVD dendrite morphogenesis
defects in rab-10 deletion mutants.
{ECO:0000269|PubMed:16394106,
ECO:0000269|PubMed:20573983,
ECO:0000269|PubMed:23100538,
ECO:0000269|PubMed:23185324,
ECO:0000269|PubMed:25301900,
ECO:0000269|PubMed:26393361,
ECO:0000269|PubMed:26394140,
ECO:0000269|PubMed:26633194}.
SEQUENCE 201 AA; 22712 MW; 2D205ABF751EBF1A CRC64;
MARRPYDMLF KLLLIGDSGV GKTCILYRFS DDAFNTTFIS TIGIDFKIKT IELKGKKIKL
QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNAKSFDNI AKWLRNIDEH ASEDVVKMIL
GNKCDMSDRR VVSRERGEKI AQDHGISFHE TSAKLNVHVD TAFYDLAEAI LAKMPDSTDE
QSRDTVNPVQ PQRQSSSGGC C


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EIAAB38042 Frizzled-related protein 1b,FRP1B,FRP-1b,Homo sapiens,Human,SARP3,SARP-3,Secreted apoptosis-related protein 3,Secreted frizzled-related protein 5,SFRP5,sFRP-5
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EIAAB12793 ELK3,ETS domain-containing protein Elk-3,ETS-related protein ERP,ETS-related protein NET,Homo sapiens,Human,NET,SAP2,SAP-2,Serum response factor accessory protein 2,SRF accessory protein 2
EIAAB08778 COX7A2L,COX7AR,COX7a-related protein,COX7RP,Cytochrome c oxidase subunit 7A-related protein, mitochondrial,Cytochrome c oxidase subunit VIIa-related protein,EB1,Homo sapiens,Human
EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29228 Homo sapiens,Human,ORP11,ORP-11,OSBP12,OSBPL11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB33753 C21KG,G-22K,GTP-binding protein smg p21A,Homo sapiens,Human,KREV1,RAP1A,Ras-related protein Krev-1,Ras-related protein Rap-1A
EIAAB29236 Homo sapiens,Human,KIAA0704,ORP3,ORP-3,OSBP3,OSBPL3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29242 Homo sapiens,Human,KIAA1451,ORP8,ORP-8,OSBP10,OSBPL8,OSBP-related protein 8,Oxysterol-binding protein-related protein 8
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
18-003-42229 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg Protein A
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.05 mg
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg
EIAAB29240 Homo sapiens,Human,ORP6,ORP-6,OSBPL6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6
EIAAB29241 Homo sapiens,Human,ORP7,ORP-7,OSBPL7,OSBP-related protein 7,Oxysterol-binding protein-related protein 7


 

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