RBCC

Full text data of PRAF2

PRAF2 [Confidence: low (only semi-automatic identification from reviews)]
PRA1 family protein 2

UniProt O60831
ID PRAF2_HUMAN Reviewed; 178 AA.
AC O60831; B2RD20;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=PRA1 family protein 2;
GN Name=PRAF2; ORFNames=JM4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CCR5.
RX PubMed=15757671; DOI=10.1016/j.febslet.2005.02.037;
RA Schweneker M., Bachmann A.S., Moelling K.;
RT "JM4 is a four-transmembrane protein binding to the CCR5 receptor.";
RL FEBS Lett. 579:1751-1758(2005).
RN [7]
RP GENOMIC ORGANIZATION, AND TISSUE SPECIFICITY.
RX PubMed=16481131; DOI=10.1016/j.gene.2005.12.009;
RA Fo C.S., Coleman C.S., Wallick C.J., Vine A.L., Bachmann A.S.;
RT "Genomic organization, expression profile, and characterization of the
RT new protein PRA1 domain family, member 2 (PRAF2).";
RL Gene 371:154-165(2006).
RN [8]
RP INTERACTION WITH GDE1.
RX PubMed=16472945; DOI=10.1016/j.gene.2005.11.023;
RA Bachmann A.S., Duennebier F.F., Mocz G.;
RT "Genomic organization, characterization, and molecular 3D model of
RT GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase.";
RL Gene 371:144-153(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17975142; DOI=10.1158/1078-0432.CCR-07-0829;
RA Geerts D., Wallick C.J., Koomoa D.-L., Koster J., Versteeg R.,
RA Go R.C.V., Bachmann A.S.;
RT "Expression of prenylated Rab acceptor 1 domain family, member 2
RT (PRAF2) in neuroblastoma: correlation with clinical features, cellular
RT localization, and cerulenin-mediated apoptosis regulation.";
RL Clin. Cancer Res. 13:6312-6319(2007).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18395978; DOI=10.1016/j.neulet.2008.03.030;
RA Koomoa D.-L., Go R.C.V., Wester K., Bachmann A.S.;
RT "Expression profile of PRAF2 in the human brain and enrichment in
RT synaptic vesicles.";
RL Neurosci. Lett. 436:171-176(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be involved in ER/Golgi transport and vesicular
CC traffic. Plays a proapoptic role in cerulenin-induced
CC neuroblastoma apoptosis.
CC -!- SUBUNIT: Interacts with CCR5 and GDE1.
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane
CC protein (Probable).
CC -!- TISSUE SPECIFICITY: Strong expression in the brain, small
CC intestine, lung, spleen, and pancreas as well as in tumor tissues
CC of the breast, colon, lung and ovary, with a weaker expression in
CC normal tissues of the same patient. High expression in
CC neuroblastic tumors. Strongly expressed in Purkinje cells and more
CC moderately in cells of the molecular and the granular layers in
CC the cerebellum. Detected in neuronal cells, but not in non-
CC neuronal cells in the cerebral cortex, hippocampus, and lateral
CC ventricles.
CC -!- SIMILARITY: Belongs to the PRA1 family.
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DR EMBL; AJ005896; CAA06753.1; -; mRNA.
DR EMBL; CR457023; CAG33304.1; -; mRNA.
DR EMBL; AK315374; BAG37767.1; -; mRNA.
DR EMBL; CH471224; EAW50706.1; -; Genomic_DNA.
DR EMBL; BC021213; AAH21213.1; -; mRNA.
DR RefSeq; NP_009144.1; NM_007213.2.
DR UniGene; Hs.29595; -.
DR ProteinModelPortal; O60831; -.
DR IntAct; O60831; 2.
DR MINT; MINT-1339907; -.
DR STRING; 9606.ENSP00000365570; -.
DR PaxDb; O60831; -.
DR PeptideAtlas; O60831; -.
DR PRIDE; O60831; -.
DR Ensembl; ENST00000376390; ENSP00000365570; ENSG00000243279.
DR GeneID; 11230; -.
DR KEGG; hsa:11230; -.
DR UCSC; uc004dmi.3; human.
DR CTD; 11230; -.
DR GeneCards; GC0XM048928; -.
DR HGNC; HGNC:28911; PRAF2.
DR HPA; CAB011655; -.
DR HPA; HPA002859; -.
DR MIM; 300840; gene.
DR neXtProt; NX_O60831; -.
DR PharmGKB; PA134955002; -.
DR eggNOG; NOG288107; -.
DR HOGENOM; HOG000231363; -.
DR HOVERGEN; HBG053661; -.
DR InParanoid; O60831; -.
DR OMA; RRFRRNH; -.
DR OrthoDB; EOG7VDXQH; -.
DR PhylomeDB; O60831; -.
DR ChiTaRS; PRAF2; human.
DR GenomeRNAi; 11230; -.
DR NextBio; 42738; -.
DR PRO; PR:O60831; -.
DR ArrayExpress; O60831; -.
DR Bgee; O60831; -.
DR CleanEx; HS_PRAF2; -.
DR Genevestigator; O60831; -.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015813; P:L-glutamate transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004895; Prenylated_rab_accept_PRA1.
DR Pfam; PF03208; PRA1; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 178 PRA1 family protein 2.
FT /FTId=PRO_0000220881.
FT TOPO_DOM 1 41 Cytoplasmic (Potential).
FT TRANSMEM 42 62 Helical; (Potential).
FT TOPO_DOM 63 64 Extracellular (Potential).
FT TRANSMEM 65 85 Helical; (Potential).
FT TOPO_DOM 86 96 Cytoplasmic (Potential).
FT TRANSMEM 97 119 Helical; (Potential).
FT TOPO_DOM 120 122 Extracellular (Potential).
FT TRANSMEM 123 140 Helical; (Potential).
FT TOPO_DOM 141 178 Cytoplasmic (Potential).
FT VARIANT 56 56 L -> F (in dbSNP:rs34565429).
FT /FTId=VAR_050628.
SQ SEQUENCE 178 AA; 19258 MW; E62695D7DC40550A CRC64;
MSEVRLPPLR ALDDFVLGSA RLAAPDPCDP QRWCHRVINN LLYYQTNYLL CFGIGLALAG
YVRPLHTLLS ALVVAVALGV LVWAAETRAA VRRCRRSHPA ACLAAVLAVG LLVLWVAGGA
CTFLFSIAGP VLLILVHASL RLRNLKNKIE NKIESIGLKR TPMGLLLEAL GQEQEAGS
//

MIM 300840
*RECORD*
*FIELD* NO
300840
*FIELD* TI
*300840 PRA1 DOMAIN FAMILY, MEMBER 2; PRAF2
;;JM4
*FIELD* TX

DESCRIPTION

PRAF2 belongs to the prenylated RAB acceptor-1 (PRA1, or RABAC1; 604925)
read moredomain family (PRAF). Members of this family have 4 transmembrane
domains, hydrophilic N and C termini, and a PRA1 domain. PRAF proteins
are involved in multiple cellular processes, including endo- and
exocytic vesicle trafficking and glutamate uptake (summary by Borsics et
al., 2010).

CLONING

Using a yeast 2-hybrid screen of a B-cell cDNA library with the C
terminus of CCR5 (601373) as bait, followed by database analysis,
Schweneker et al. (2005) identified PRAF2, which they called JM4
(Jena-Muenchen-4). The predicted 178-amino acid protein contains 4
transmembrane-spanning domains and is evolutionarily conserved. It
shares 42% amino acid identity, as well as structural similarity, with
JWA (ARL6IP5; 605709). Northern blot analysis revealed near ubiquitous
expression of a 1.2-kb transcript in human tissues. Cell fractionation
and Western blot analysis showed association of JM4 with cellular
membranes in transfected canine thymocytes. Confocal microscopy
demonstrated colocalization of JM4 with JWA, as well as with calnexin
(CANX; 114217), an endoplasmic reticulum marker, and M6PR (154540), a
trans-Golgi network and endosome marker, in granular structures of
transfected HeLa and COS cells.

Fo et al. (2006) determined that the human PRAF2 protein contains an
N-terminal amphiphysin (AMPH; 600418) SH3 domain, 4 transmembrane
domains, intracellular N and C termini, and 2 putative phosphorylation
sites. Western blot analysis showed that PRAF2 was expressed as a 19-kD
protein, consistent with its calculated molecular mass, in all human
tissues examined except testis. Strongest expression was detected in
brain, small intestine, lung, spleen, and pancreas. Possible dimer
formation and/or posttranslational modifications were observed in
several tissues.

By immunohistochemical analysis, Koomoa et al. (2008) found strong PRAF2
expression in Purkinje cells in human cerebellum, with more moderate
expression in cells of the molecular and granular levels. Expression in
human cerebral cortex, hippocampus, and lateral ventricles was
restricted to neuronal cells. Immunoblot analysis showed expression of
Praf2 in synaptic vesicles of rat brain.

GENE FUNCTION

By coimmunoprecipitation analysis of transfected HEK293 cells,
Schweneker et al. (2005) confirmed that JM4 interacted with CCR5. JM4
formed dimers and trimers with itself and heteromultimers with human and
rat JWA in transfected cells. Schweneker et al. (2005) concluded that
JM4 is a CCR5-interacting protein that may function in trafficking and
membrane localization of CCR5 and other receptors.

Using immunohistochemical analysis, Fo et al. (2006) showed that PRAF2
was overexpressed in human breast, colon, lung, and ovary cancer tissues
compared with corresponding normal tissues.

Using microarray analysis, Geerts et al. (2007) detected PRAF2 mRNA in
most tumor types examined, with highest expression in pediatric
neuroblastic tumors (see 256700). In neuroblastoma patients, PRAF2
expression correlated with higher patient age (greater than 1 year),
poorer patient survival, higher stage tumors, and MYCN (164840)
amplification. Immunofluorescence microscopy of neuroblastoma cells
demonstrated localization of PRAF2 in cytoplasmic punctae, with weaker
expression in nuclei and perinuclear regions. Treatment of neuroblastoma
cells with cerulenin, a fungal metabolite, further increased PRAF2
expression, followed by loss of spindle-like morphology and the onset of
rounding and apoptosis. Geerts et al. (2007) concluded that increased
expression of PRAF2, which is associated with clinical features
predicting unfavorable disease outcome, is a candidate prognostic marker
in neuroblastoma.

Using microarray and immunoblot analyses and immunofluorescence
microscopy, Borsics et al. (2010) demonstrated elevated expression of
PRAF2 mRNA and protein in multiple cancer types, with highest expression
in malignant glioma. Subcellular expression was high in small,
cytoplasmic vesicle-like structures, as well as in and around nuclei, of
a malignant glioma cell line. Monomeric 19-kD PRAF2 was associated with
nuclear fractions and nuclear and cytoplasmic membranes, whereas 37-kD
dimeric forms of PRAF2 were found in cytosol. Knockdown of PRAF2 reduced
the viability of the glioblastoma cell line and inhibited migration and
invasion.

GENE STRUCTURE

Fo et al. (2006) determined that the PRAF2 gene contains 3 exons and
spans about 2.8 kb.

MAPPING

By genomic sequence analysis, Fo et al. (2006) mapped the PRAF2 gene to
chromosome Xp11.23.

*FIELD* RF
1. Borsics, T.; Lundberg, E.; Geerts, D.; Koomoa, D.-L. T.; Koster,
J.; Wester, K.; Bachmann, A. S.: Subcellular distribution and expression
of prenylated Rab acceptor 1 domain family, member 2 (PRAF2) in malignant
glioma: influence on cell survival and migration. Cancer Sci. 101:
1624-1631, 2010.

2. Fo, C. S.; Coleman, C. S.; Wallick, C. J.; Vine, A. L.; Bachmann,
A. S.: Genomic organization, expression profile, and characterization
of the new protein PRA1 domain family, member 2 (PRAF2). Gene 371:
154-165, 2006.

3. Geerts, D.; Wallick, C. J.; Koomoa, D.-L. T.; Koster, J.; Versteeg,
R.; Go, R. C. V.; Bachmann, A. S.: Expression of prenylated Rab acceptor
1 domain family, member 2 (PRAF2) in neuroblastoma: correlation with
clinical features, cellular localization, and cerulenin-mediated apoptosis
regulation. Clin. Cancer Res. 13: 6312-6319, 2007.

4. Koomoa, D.-L. T.; Go, R. C. V.; Wester, K.; Bachmann, A. S.: Expression
profile of PRAF2 in the human brain and enrichment in synaptic vesicles. Neurosci.
Lett. 436: 171-176, 2008.

5. Schweneker, M.; Bachmann, A. S.; Moelling, K.: JM4 is a four-transmembrane
protein binding to the CCR5 receptor. FEBS Lett. 579: 1751-1758,
2005.

*FIELD* CD
Paul J. Converse: 3/29/2011

*FIELD* ED
mgross: 03/29/2011

RBCC Red Blood Cell Collection

Full text data of PRAF2