Full text data of PTPLAD1
PTPLAD1
(BIND1, HACD3)
[Confidence: high (present in two of the MS resources)]
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3; 4.2.1.134 (3-hydroxyacyl-CoA dehydratase 3; HACD3; Butyrate-induced protein 1; B-ind1; hB-ind1; Protein tyrosine phosphatase-like protein PTPLAD1; Protein-tyrosine phosphatase-like A domain-containing protein 1)
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3; 4.2.1.134 (3-hydroxyacyl-CoA dehydratase 3; HACD3; Butyrate-induced protein 1; B-ind1; hB-ind1; Protein tyrosine phosphatase-like protein PTPLAD1; Protein-tyrosine phosphatase-like A domain-containing protein 1)
UniProt
Q9P035
ID HACD3_HUMAN Reviewed; 362 AA.
AC Q9P035; A0PJA1; Q280Z3; Q6PD63; Q8IUI5; Q8NC86; Q8NCB1; Q96T12;
read moreAC Q9NQA7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3;
DE EC=4.2.1.134;
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 3;
DE Short=HACD3;
DE AltName: Full=Butyrate-induced protein 1;
DE Short=B-ind1;
DE Short=hB-ind1;
DE AltName: Full=Protein tyrosine phosphatase-like protein PTPLAD1;
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1;
GN Name=PTPLAD1; Synonyms=BIND1, HACD3;
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 [MRNA], FUNCTION, INTERACTION WITH RAC1, AND
RP TISSUE SPECIFICITY.
RX PubMed=10747961; DOI=10.1074/jbc.M000887200;
RA Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.;
RT "B-ind1, a novel mediator of Rac1 signaling cloned from sodium
RT butyrate-treated fibroblasts.";
RL J. Biol. Chem. 275:17344-17348(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=B-cell, Duodenum, Eye, and Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=16516406; DOI=10.1016/j.gene.2006.01.022;
RA Sabbah M., Saucier C., Redeuilh G.;
RT "Human B-ind1 gene promoter: cloning and regulation by histone
RT deacetylase inhibitors.";
RL Gene 374:128-133(2006).
RN [6]
RP INDUCTION BY AKAP12.
RX PubMed=16638134; DOI=10.1186/1471-2407-6-105;
RA Liu Y., Gao L., Gelman I.H.;
RT "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and
RT angiogenic genes during suppression of v-Src-induced oncogenesis.";
RL BMC Cancer 6:105-105(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ELOVL FAMILY.
RX PubMed=18554506; DOI=10.1016/j.febslet.2008.06.007;
RA Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y.,
RA Igarashi Y., Kihara A.;
RT "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases
RT involved in very long-chain fatty acid synthesis.";
RL FEBS Lett. 582:2435-2440(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Responsible for the dehydration step in very long-chain
CC fatty acid (VLCFA) synthesis. Involved in Rac1-signaling pathways
CC leading to the modulation of gene expression.
CC -!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-[acyl-
CC carrier protein] = a very-long-chain trans-2,3-dehydroacyl-[acyl-
CC carrier protein] + H(2)O.
CC -!- SUBUNIT: Interacts with the condensation enzymes of the ELOVL
CC family. Interacts with RAC1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, kidney, brain,
CC liver and weakly in skeletal muscle, spleen and heart. No
CC expression detected in leukocytes.
CC -!- INDUCTION: By AKAP12 and histone deacetylase inhibitors such as
CC sodium butyrate.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase
CC HACD family.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29085.1; Type=Frameshift; Positions=356;
CC Sequence=BAC11249.1; Type=Frameshift; Positions=359;
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DR EMBL; AJ271091; CAB69070.1; -; mRNA.
DR EMBL; AF161470; AAF29085.1; ALT_FRAME; mRNA.
DR EMBL; AK027421; BAB55101.1; -; mRNA.
DR EMBL; AK074857; BAC11249.1; ALT_FRAME; mRNA.
DR EMBL; AK074898; BAC11277.1; -; mRNA.
DR EMBL; BC019873; AAH19873.1; -; mRNA.
DR EMBL; BC035508; AAH35508.1; -; mRNA.
DR EMBL; BC047685; AAH47685.1; -; mRNA.
DR EMBL; BC058912; AAH58912.1; -; mRNA.
DR EMBL; DQ251107; ABB83547.1; -; Genomic_DNA.
DR RefSeq; NP_057479.2; NM_016395.2.
DR UniGene; Hs.512973; -.
DR ProteinModelPortal; Q9P035; -.
DR SMR; Q9P035; 5-158.
DR IntAct; Q9P035; 13.
DR MINT; MINT-1135933; -.
DR PhosphoSite; Q9P035; -.
DR DMDM; 166199462; -.
DR PaxDb; Q9P035; -.
DR PRIDE; Q9P035; -.
DR Ensembl; ENST00000261875; ENSP00000261875; ENSG00000074696.
DR GeneID; 51495; -.
DR KEGG; hsa:51495; -.
DR UCSC; uc002apc.3; human.
DR CTD; 51495; -.
DR GeneCards; GC15P065822; -.
DR H-InvDB; HIX0012353; -.
DR HGNC; HGNC:24175; PTPLAD1.
DR HPA; HPA014837; -.
DR neXtProt; NX_Q9P035; -.
DR PharmGKB; PA142671113; -.
DR eggNOG; COG5198; -.
DR HOVERGEN; HBG108301; -.
DR InParanoid; Q9P035; -.
DR OrthoDB; EOG7BP82H; -.
DR ChiTaRS; PTPLAD1; human.
DR GeneWiki; PTPLAD1; -.
DR GenomeRNAi; 51495; -.
DR NextBio; 55161; -.
DR PRO; PR:Q9P035; -.
DR ArrayExpress; Q9P035; -.
DR Bgee; Q9P035; -.
DR CleanEx; HS_PTPLAD1; -.
DR Genevestigator; Q9P035; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:ProtInc.
DR GO; GO:0016601; P:Rac protein signal transduction; NAS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 362 Very-long-chain (3R)-3-hydroxyacyl-[acyl-
FT carrier protein] dehydratase 3.
FT /FTId=PRO_0000313724.
FT TOPO_DOM 1 149 Cytoplasmic (Potential).
FT TRANSMEM 150 170 Helical; (Potential).
FT TOPO_DOM 171 185 Lumenal (Potential).
FT TRANSMEM 186 207 Helical; (Potential).
FT TOPO_DOM 208 217 Cytoplasmic (Potential).
FT TRANSMEM 218 235 Helical; (Potential).
FT TOPO_DOM 236 241 Lumenal (Potential).
FT TRANSMEM 242 256 Helical; (Potential).
FT TOPO_DOM 257 279 Cytoplasmic (Potential).
FT TRANSMEM 280 298 Helical; (Potential).
FT TOPO_DOM 299 322 Lumenal (Potential).
FT TRANSMEM 323 343 Helical; (Potential).
FT TOPO_DOM 344 362 Cytoplasmic (Potential).
FT DOMAIN 5 94 CS.
FT COILED 111 136 Potential.
FT COMPBIAS 350 353 Poly-Arg.
FT COMPBIAS 357 360 Poly-Lys.
FT ACT_SITE 286 286 By similarity.
FT ACT_SITE 293 293 By similarity.
FT MOD_RES 114 114 Phosphoserine.
FT VARIANT 56 56 E -> K (in dbSNP:rs11632737).
FT /FTId=VAR_037712.
FT VARIANT 269 269 M -> L (in dbSNP:rs2279854).
FT /FTId=VAR_037713.
FT CONFLICT 60 60 E -> K (in Ref. 3; BAB55101).
FT CONFLICT 245 245 F -> I (in Ref. 3; BAC11277).
FT CONFLICT 282 282 W -> G (in Ref. 4; AAH35508).
FT CONFLICT 292 292 A -> V (in Ref. 2; AAF29085).
FT CONFLICT 352 362 RRYGQKKKKIH -> LKMRAGAVAHACDPSALGG (in
FT Ref. 1; CAB69070).
FT CONFLICT 361 361 I -> K (in Ref. 4; AAH35508).
SQ SEQUENCE 362 AA; 43160 MW; 1B3591E88DD85D16 CRC64;
MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE
FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
RAKEEERLNK LRLESEGSPE TLTNLRKGYL FMYNLVQFLG FSWIFVNLTV RFCILGKESF
YDTFHTVADM MYFCQMLAVV ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN
KAVVFFVFYL WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS
IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR RRRYGQKKKK
IH
//
ID HACD3_HUMAN Reviewed; 362 AA.
AC Q9P035; A0PJA1; Q280Z3; Q6PD63; Q8IUI5; Q8NC86; Q8NCB1; Q96T12;
read moreAC Q9NQA7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3;
DE EC=4.2.1.134;
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 3;
DE Short=HACD3;
DE AltName: Full=Butyrate-induced protein 1;
DE Short=B-ind1;
DE Short=hB-ind1;
DE AltName: Full=Protein tyrosine phosphatase-like protein PTPLAD1;
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1;
GN Name=PTPLAD1; Synonyms=BIND1, HACD3;
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 [MRNA], FUNCTION, INTERACTION WITH RAC1, AND
RP TISSUE SPECIFICITY.
RX PubMed=10747961; DOI=10.1074/jbc.M000887200;
RA Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.;
RT "B-ind1, a novel mediator of Rac1 signaling cloned from sodium
RT butyrate-treated fibroblasts.";
RL J. Biol. Chem. 275:17344-17348(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=B-cell, Duodenum, Eye, and Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=16516406; DOI=10.1016/j.gene.2006.01.022;
RA Sabbah M., Saucier C., Redeuilh G.;
RT "Human B-ind1 gene promoter: cloning and regulation by histone
RT deacetylase inhibitors.";
RL Gene 374:128-133(2006).
RN [6]
RP INDUCTION BY AKAP12.
RX PubMed=16638134; DOI=10.1186/1471-2407-6-105;
RA Liu Y., Gao L., Gelman I.H.;
RT "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and
RT angiogenic genes during suppression of v-Src-induced oncogenesis.";
RL BMC Cancer 6:105-105(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INTERACTION WITH ELOVL FAMILY.
RX PubMed=18554506; DOI=10.1016/j.febslet.2008.06.007;
RA Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y.,
RA Igarashi Y., Kihara A.;
RT "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases
RT involved in very long-chain fatty acid synthesis.";
RL FEBS Lett. 582:2435-2440(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Responsible for the dehydration step in very long-chain
CC fatty acid (VLCFA) synthesis. Involved in Rac1-signaling pathways
CC leading to the modulation of gene expression.
CC -!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-[acyl-
CC carrier protein] = a very-long-chain trans-2,3-dehydroacyl-[acyl-
CC carrier protein] + H(2)O.
CC -!- SUBUNIT: Interacts with the condensation enzymes of the ELOVL
CC family. Interacts with RAC1.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, kidney, brain,
CC liver and weakly in skeletal muscle, spleen and heart. No
CC expression detected in leukocytes.
CC -!- INDUCTION: By AKAP12 and histone deacetylase inhibitors such as
CC sodium butyrate.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase
CC HACD family.
CC -!- SIMILARITY: Contains 1 CS domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29085.1; Type=Frameshift; Positions=356;
CC Sequence=BAC11249.1; Type=Frameshift; Positions=359;
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DR EMBL; AJ271091; CAB69070.1; -; mRNA.
DR EMBL; AF161470; AAF29085.1; ALT_FRAME; mRNA.
DR EMBL; AK027421; BAB55101.1; -; mRNA.
DR EMBL; AK074857; BAC11249.1; ALT_FRAME; mRNA.
DR EMBL; AK074898; BAC11277.1; -; mRNA.
DR EMBL; BC019873; AAH19873.1; -; mRNA.
DR EMBL; BC035508; AAH35508.1; -; mRNA.
DR EMBL; BC047685; AAH47685.1; -; mRNA.
DR EMBL; BC058912; AAH58912.1; -; mRNA.
DR EMBL; DQ251107; ABB83547.1; -; Genomic_DNA.
DR RefSeq; NP_057479.2; NM_016395.2.
DR UniGene; Hs.512973; -.
DR ProteinModelPortal; Q9P035; -.
DR SMR; Q9P035; 5-158.
DR IntAct; Q9P035; 13.
DR MINT; MINT-1135933; -.
DR PhosphoSite; Q9P035; -.
DR DMDM; 166199462; -.
DR PaxDb; Q9P035; -.
DR PRIDE; Q9P035; -.
DR Ensembl; ENST00000261875; ENSP00000261875; ENSG00000074696.
DR GeneID; 51495; -.
DR KEGG; hsa:51495; -.
DR UCSC; uc002apc.3; human.
DR CTD; 51495; -.
DR GeneCards; GC15P065822; -.
DR H-InvDB; HIX0012353; -.
DR HGNC; HGNC:24175; PTPLAD1.
DR HPA; HPA014837; -.
DR neXtProt; NX_Q9P035; -.
DR PharmGKB; PA142671113; -.
DR eggNOG; COG5198; -.
DR HOVERGEN; HBG108301; -.
DR InParanoid; Q9P035; -.
DR OrthoDB; EOG7BP82H; -.
DR ChiTaRS; PTPLAD1; human.
DR GeneWiki; PTPLAD1; -.
DR GenomeRNAi; 51495; -.
DR NextBio; 55161; -.
DR PRO; PR:Q9P035; -.
DR ArrayExpress; Q9P035; -.
DR Bgee; Q9P035; -.
DR CleanEx; HS_PTPLAD1; -.
DR Genevestigator; Q9P035; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; TAS:ProtInc.
DR GO; GO:0016601; P:Rac protein signal transduction; NAS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Membrane; Phosphoprotein; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 362 Very-long-chain (3R)-3-hydroxyacyl-[acyl-
FT carrier protein] dehydratase 3.
FT /FTId=PRO_0000313724.
FT TOPO_DOM 1 149 Cytoplasmic (Potential).
FT TRANSMEM 150 170 Helical; (Potential).
FT TOPO_DOM 171 185 Lumenal (Potential).
FT TRANSMEM 186 207 Helical; (Potential).
FT TOPO_DOM 208 217 Cytoplasmic (Potential).
FT TRANSMEM 218 235 Helical; (Potential).
FT TOPO_DOM 236 241 Lumenal (Potential).
FT TRANSMEM 242 256 Helical; (Potential).
FT TOPO_DOM 257 279 Cytoplasmic (Potential).
FT TRANSMEM 280 298 Helical; (Potential).
FT TOPO_DOM 299 322 Lumenal (Potential).
FT TRANSMEM 323 343 Helical; (Potential).
FT TOPO_DOM 344 362 Cytoplasmic (Potential).
FT DOMAIN 5 94 CS.
FT COILED 111 136 Potential.
FT COMPBIAS 350 353 Poly-Arg.
FT COMPBIAS 357 360 Poly-Lys.
FT ACT_SITE 286 286 By similarity.
FT ACT_SITE 293 293 By similarity.
FT MOD_RES 114 114 Phosphoserine.
FT VARIANT 56 56 E -> K (in dbSNP:rs11632737).
FT /FTId=VAR_037712.
FT VARIANT 269 269 M -> L (in dbSNP:rs2279854).
FT /FTId=VAR_037713.
FT CONFLICT 60 60 E -> K (in Ref. 3; BAB55101).
FT CONFLICT 245 245 F -> I (in Ref. 3; BAC11277).
FT CONFLICT 282 282 W -> G (in Ref. 4; AAH35508).
FT CONFLICT 292 292 A -> V (in Ref. 2; AAF29085).
FT CONFLICT 352 362 RRYGQKKKKIH -> LKMRAGAVAHACDPSALGG (in
FT Ref. 1; CAB69070).
FT CONFLICT 361 361 I -> K (in Ref. 4; AAH35508).
SQ SEQUENCE 362 AA; 43160 MW; 1B3591E88DD85D16 CRC64;
MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE
FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
RAKEEERLNK LRLESEGSPE TLTNLRKGYL FMYNLVQFLG FSWIFVNLTV RFCILGKESF
YDTFHTVADM MYFCQMLAVV ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN
KAVVFFVFYL WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS
IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR RRRYGQKKKK
IH
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