Документ взят из кэша поисковой машины. Адрес оригинального документа : http://kodomo.cmm.msu.ru/~robo_tema/Term4/c43bp_human.entret Дата изменения: Wed May 13 16:36:56 2009 Дата индексирования: Tue Oct 2 14:39:10 2012 Кодировка: Поисковые слова: massive stars

ID C43BP_HUMAN Reviewed; 624 AA.
AC Q9Y5P4; Q53YV1; Q53YV2; Q96Q85; Q96Q88; Q9H2S7; Q9H2S8;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-MAR-2009, entry version 69.
DE RecName: Full=Collagen type IV alpha-3-binding protein;
DE AltName: Full=Ceramide transfer protein;
DE Short=hCERT;
DE AltName: Full=Goodpasture antigen-binding protein;
DE Short=GPBP;
DE AltName: Full=StAR-related lipid transfer protein 11;
DE AltName: Full=START domain-containing protein 11;
DE Short=StARD11;
GN Name=COL4A3BP; Synonyms=CERT, STARD11;
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] (ISOFORM 1), AND CHARACTERIZATION.
RX MEDLINE=99230287; PubMed=10212244; DOI=10.1074/jbc.274.18.12642;
RA Raya A., Revert F., Navarro S., Saus J.;
RT "Characterization of a novel type of serine/threonine kinase that
RT specifically phosphorylates the human goodpasture antigen.";
RL J. Biol. Chem. 274:12642-12649(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX MEDLINE=20568301; PubMed=11007769; DOI=10.1074/jbc.M002769200;
RA Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E.,
RA Vieites B., Granero F., Forteza J., Saus J.;
RT "Goodpasture antigen-binding protein, the kinase that phosphorylates
RT the Goodpasture antigen, is an alternatively spliced variant
RT implicated in autoimmune pathogenesis.";
RL J. Biol. Chem. 275:40392-40399(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DOMAIN,
RP SUBCELLULAR LOCATION, AND VARIANT GLU-67.
RX PubMed=14685229; DOI=10.1038/nature02188;
RA Hanada K., Kumagai K., Yasuda S., Miura Y., Kawano M., Fukasawa M.,
RA Nishijima M.;
RT "Molecular machinery for non-vesicular trafficking of ceramide.";
RL Nature 426:803-809(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RA Ogi T., Yamamoto Y., Ohmori H.;
RT "Homo sapiens genomic sequence, containing DINB1 and GPBP gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS
RP SPECTROMETRY.
RC TISSUE=Epithelium;
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 INTERACTION WITH VAPA AND VAPB, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASP-324.
RX PubMed=16895911; DOI=10.1074/jbc.M605032200;
RA Kawano M., Kumagai K., Nishijima M., Hanada K.;
RT "Efficient trafficking of ceramide from the endoplasmic reticulum to
RT the Golgi apparatus requires a VAMP-associated protein-interacting
RT FFAT motif of CERT.";
RL J. Biol. Chem. 281:30279-30288(2006).
RN [9]
RP PHOSPHORYLATION AT SER-132, FUNCTION, AND MUTAGENESIS OF SER-132.
RX PubMed=17591919; DOI=10.1083/jcb.200612017;
RA Fugmann T., Hausser A., Schoeffler P., Schmid S., Pfizenmaier K.,
RA Olayioye M.A.;
RT "Regulation of secretory transport by protein kinase D-mediated
RT phosphorylation of the ceramide transfer protein.";
RL J. Cell Biol. 178:15-22(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASS
RP SPECTROMETRY.
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).
CC -!- FUNCTION: May mediate the intracellular trafficking of ceramide in
CC a non-vesicular manner.
CC -!- SUBUNIT: Interacts with COL4A3. Interacts with VAPA and VAPB.
CC Interaction with VAPB is less efficient than with VAPA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Endoplasmic
CC reticulum. Note=Preferentially localized to the Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CERTL;
CC IsoId=Q9Y5P4-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta26, GPBPD26;
CC IsoId=Q9Y5P4-2; Sequence=VSP_006276;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The START domain recognizes ceramide and mediates the
CC intermembrane transfer of ceramide.
CC -!- DOMAIN: The PH domain targets the Golgi apparatus.
CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA and
CC VAPB.
CC -!- PTM: Phosphorylation on Ser-132 decreases the affinity toward
CC phosphatidylinositol 4-phosphate at Golgi membranes and reduces
CC ceramide transfer activity.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 START domain.
CC -!- CAUTION: Was originally (PubMed:10212244) reported to have a
CC protein kinase activity and to phosphorylates on Ser and Thr
CC residues the Goodpasture autoantigen (in vitro).
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DR EMBL; AF136450; AAD30288.1; -; mRNA.
DR EMBL; AF232930; AAG42046.1; -; mRNA.
DR EMBL; AF232935; AAG42051.1; -; Genomic_DNA.
DR EMBL; AY453385; AAR26717.1; -; mRNA.
DR EMBL; AY453386; AAR26718.1; -; mRNA.
DR EMBL; AK091851; BAC03762.1; -; mRNA.
DR EMBL; BC000102; AAH00102.1; -; mRNA.
DR EMBL; AB036934; BAB58974.1; -; Genomic_DNA.
DR EMBL; AB036936; BAB58977.1; -; Genomic_DNA.
DR IPI; IPI00024701; -.
DR IPI; IPI00182914; -.
DR RefSeq; NP_005704.1; -.
DR UniGene; Hs.270437; -.
DR IntAct; Q9Y5P4; 6.
DR PhosphoSite; Q9Y5P4; -.
DR PRIDE; Q9Y5P4; -.
DR Ensembl; ENSG00000113163; Homo sapiens.
DR GeneID; 10087; -.
DR KEGG; hsa:10087; -.
DR GeneCards; GC05M074705; -.
DR H-InvDB; HIX0004955; -.
DR HGNC; HGNC:2205; COL4A3BP.
DR MIM; 604677; gene.
DR PharmGKB; PA26720; -.
DR HOGENOM; Q9Y5P4; -.
DR HOVERGEN; Q9Y5P4; -.
DR BRENDA; 2.7.11.9; 247.
DR NextBio; 38145; -.
DR ArrayExpress; Q9Y5P4; -.
DR Bgee; Q9Y5P4; -.
DR CleanEx; HS_COL4A3BP; -.
DR GermOnline; ENSG00000113163; Homo sapiens.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc.
DR InterPro; IPR011993; PH_type.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR002913; START_lipid_bd.
DR Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Phosphoprotein; Transport.
FT CHAIN 1 624 Collagen type IV alpha-3-binding protein.
FT /FTId=PRO_0000220665.
FT DOMAIN 23 117 PH.
FT DOMAIN 389 618 START.
FT COILED 263 303 Potential.
FT MOTIF 321 327 FFAT.
FT MOD_RES 132 132 Phosphoserine; by PKD.
FT MOD_RES 315 315 Phosphoserine.
FT MOD_RES 377 377 Phosphoserine.
FT MOD_RES 380 380 Phosphoserine (By similarity).
FT MOD_RES 611 611 Phosphoserine (By similarity).
FT VAR_SEQ 371 396 Missing (in isoform 2).
FT /FTId=VSP_006276.
FT VARIANT 67 67 G -> E (in LY-A cell line; destroyes the
FT phosphatidylinositol 4-phosphate-binding
FT activity).
FT /FTId=VAR_035416.
FT MUTAGEN 132 132 S->A: Abolishes the phosphorylation.
FT Strongly reduces the interaction with
FT phosphatidylinositol 4-phosphate.
FT Increases the ceramide transfer activity.
FT MUTAGEN 324 324 D->A: Impairs the endoplasmic reticulum-
FT to-Golgi ceramide trafficking and
FT abolishes the interaction with VAPA.
SQ SEQUENCE 624 AA; 70835 MW; A125162492AC5A0E CRC64;
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPH VTPKGINGID
FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDAFS
SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV
VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
//