GENTAUR Molecular Products.

 CLIP3_HUMAN             Reviewed;         547 AA.
 Q96DZ5; A8K0E4; Q8WWL1; Q96C99; Q9UFT7;
 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
 17-OCT-2006, sequence version 3.
 12-SEP-2018, entry version 151.
 RecName: Full=CAP-Gly domain-containing linker protein 3;
 AltName: Full=Cytoplasmic linker protein 170-related 59 kDa protein;
          Short=CLIP-170-related 59 kDa protein;
          Short=CLIPR-59;
 Name=CLIP3; Synonyms=CLIPR59;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=11854307; DOI=10.1083/jcb.200111003;
 Perez F., Pernet-Gallay K., Nizak C., Goodson H.V., Kreis T.E.,
 Goud B.;
 "CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging
 to the CLIP-170 family.";
 J. Cell Biol. 156:631-642(2002).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Brain, and Cerebellum;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-175.
 TISSUE=Brain, and Skin;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 387-547.
 TISSUE=Uterus;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [5]
 FUNCTION, AND INTERACTION WITH AKT1 AND AKT2.
 PubMed=19139280; DOI=10.1128/MCB.00754-08;
 Ding J., Du K.;
 "ClipR-59 interacts with Akt and regulates Akt cellular
 compartmentalization.";
 Mol. Cell. Biol. 29:1459-1471(2009).
 [6]
 PALMITOYLATION AT CYS-534 AND CYS-535, SUBCELLULAR LOCATION, AND
 MUTAGENESIS OF 534-CYS--CYS-535.
 PubMed=24001771; DOI=10.1128/MCB.00527-13;
 Ren W., Sun Y., Du K.;
 "DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with
 the plasma membrane.";
 Mol. Cell. Biol. 33:4255-4265(2013).
 [7]
 INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF PRO-509.
 PubMed=26198635; DOI=10.1074/jbc.M115.657668;
 Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
 "Identification of a novel sequence motif recognized by the ankyrin
 repeat domain of zDHHC17/13 S-acyltransferases.";
 J. Biol. Chem. 290:21939-21950(2015).
 [8]
 INTERACTION WITH ZDHHC17.
 PubMed=28882895; DOI=10.1074/jbc.M117.799650;
 Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
 "Peptide array based screening reveals a large number of proteins
 interacting with the ankyrin repeat domain of the zDHHC17 S-
 acyltransferase.";
 J. Biol. Chem. 292:17190-17202(2017).
 [9]
 STRUCTURE BY NMR OF 285-366.
 RIKEN structural genomics initiative (RSGI);
 "Solution structure of the 1st CAP-GLY domain in human clip-170-
 related protein CLIPR59.";
 Submitted (NOV-2005) to the PDB data bank.
 -!- FUNCTION: Functions as a cytoplasmic linker protein. Involved in
     TGN-endosome dynamics. May modulate the cellular
     compartmentalization of AKT kinase family and promote its cell
     membrane localization, thereby playing a role in glucose transport
     in adipocytes. {ECO:0000269|PubMed:19139280}.
 -!- SUBUNIT: Homodimer. Interacts with AKT1 and AKT2; when AKT1 and
     AKT2 are phosphorylated and activated, affinity is higher for AKT2
     (PubMed:19139280). Interacts with ZDHHC13 (via ANK repeats)
     (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
     (PubMed:26198635, PubMed:28882895). {ECO:0000269|PubMed:19139280,
     ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:28882895}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24001771};
     Lipid-anchor {ECO:0000269|PubMed:24001771}. Cytoplasm
     {ECO:0000269|PubMed:24001771}. Golgi apparatus, Golgi stack
     {ECO:0000269|PubMed:24001771}. Note=Localized to Golgi stacks as
     well as on tubulovesicular elements juxtaposed to Golgi cisternae.
 -!- DOMAIN: Microtubule association is inhibited by the ANK repeats
     and the Golgi localization region (GoLD).
 -!- PTM: Palmitoylation by ZDHHC17 regulates association with the
     plasma membrane. {ECO:0000269|PubMed:24001771}.
 -!- MISCELLANEOUS: The N-terminal half is dispensable for proper Golgi
     targeting, whereas the GoLD region is required.
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 EMBL; AJ427922; CAD20873.1; -; mRNA.
 EMBL; AK094738; BAG52921.1; -; mRNA.
 EMBL; AK289509; BAF82198.1; -; mRNA.
 EMBL; BC013116; AAH13116.2; -; mRNA.
 EMBL; BC014486; AAH14486.2; -; mRNA.
 EMBL; AL117468; CAB55943.1; -; mRNA.
 CCDS; CCDS12486.1; -.
 PIR; T17253; T17253.
 RefSeq; NP_001186499.1; NM_001199570.1.
 RefSeq; NP_056341.1; NM_015526.2.
 UniGene; Hs.466539; -.
 PDB; 2CP0; NMR; -; A=285-366.
 PDBsum; 2CP0; -.
 ProteinModelPortal; Q96DZ5; -.
 SMR; Q96DZ5; -.
 BioGrid; 117475; 9.
 IntAct; Q96DZ5; 4.
 STRING; 9606.ENSP00000353732; -.
 iPTMnet; Q96DZ5; -.
 PhosphoSitePlus; Q96DZ5; -.
 SwissPalm; Q96DZ5; -.
 BioMuta; CLIP3; -.
 DMDM; 116241302; -.
 EPD; Q96DZ5; -.
 PaxDb; Q96DZ5; -.
 PeptideAtlas; Q96DZ5; -.
 PRIDE; Q96DZ5; -.
 ProteomicsDB; 76346; -.
 Ensembl; ENST00000360535; ENSP00000353732; ENSG00000105270.
 Ensembl; ENST00000593074; ENSP00000466832; ENSG00000105270.
 GeneID; 25999; -.
 KEGG; hsa:25999; -.
 UCSC; uc002ocz.3; human.
 CTD; 25999; -.
 EuPathDB; HostDB:ENSG00000105270.14; -.
 GeneCards; CLIP3; -.
 H-InvDB; HIX0040341; -.
 HGNC; HGNC:24314; CLIP3.
 MIM; 607382; gene.
 neXtProt; NX_Q96DZ5; -.
 OpenTargets; ENSG00000105270; -.
 PharmGKB; PA162382439; -.
 eggNOG; KOG4568; Eukaryota.
 eggNOG; COG5244; LUCA.
 GeneTree; ENSGT00760000119173; -.
 HOGENOM; HOG000007206; -.
 HOVERGEN; HBG057079; -.
 InParanoid; Q96DZ5; -.
 KO; K10423; -.
 OMA; ICPPKLG; -.
 OrthoDB; EOG091G04NK; -.
 PhylomeDB; Q96DZ5; -.
 TreeFam; TF326096; -.
 Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
 EvolutionaryTrace; Q96DZ5; -.
 GenomeRNAi; 25999; -.
 PRO; PR:Q96DZ5; -.
 Proteomes; UP000005640; Chromosome 19.
 Bgee; ENSG00000105270; Expressed in 189 organ(s), highest expression level in cerebellum.
 CleanEx; HS_CLIP3; -.
 ExpressionAtlas; Q96DZ5; baseline and differential.
 Genevisible; Q96DZ5; HS.
 GO; GO:0005829; C:cytosol; TAS:Reactome.
 GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
 GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
 GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
 GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
 GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
 GO; GO:0035594; F:ganglioside binding; IDA:UniProtKB.
 GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO; GO:0072321; P:chaperone-mediated protein transport; IMP:UniProtKB.
 GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
 GO; GO:0044091; P:membrane biogenesis; IMP:UniProtKB.
 GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:UniProtKB.
 GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
 GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
 GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
 GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
 GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
 GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
 CDD; cd00204; ANK; 1.
 Gene3D; 1.25.40.20; -; 1.
 Gene3D; 2.30.30.190; -; 2.
 InterPro; IPR002110; Ankyrin_rpt.
 InterPro; IPR020683; Ankyrin_rpt-contain_dom.
 InterPro; IPR036770; Ankyrin_rpt-contain_sf.
 InterPro; IPR036859; CAP-Gly_dom_sf.
 InterPro; IPR000938; CAP-Gly_domain.
 Pfam; PF12796; Ank_2; 1.
 Pfam; PF01302; CAP_GLY; 2.
 SMART; SM00248; ANK; 3.
 SMART; SM01052; CAP_GLY; 2.
 SUPFAM; SSF48403; SSF48403; 1.
 SUPFAM; SSF74924; SSF74924; 2.
 PROSITE; PS50297; ANK_REP_REGION; 1.
 PROSITE; PS50088; ANK_REPEAT; 1.
 PROSITE; PS00845; CAP_GLY_1; 2.
 PROSITE; PS50245; CAP_GLY_2; 2.
 1: Evidence at protein level;
 3D-structure; ANK repeat; Cell membrane; Complete proteome; Cytoplasm;
 Golgi apparatus; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
 Polymorphism; Reference proteome; Repeat.
 CHAIN         1    547       CAP-Gly domain-containing linker protein
                              3.
                              /FTId=PRO_0000076212.
 REPEAT      117    158       ANK 1.
 REPEAT      160    191       ANK 2.
 REPEAT      197    229       ANK 3.
 DOMAIN      314    356       CAP-Gly 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00045}.
 DOMAIN      436    478       CAP-Gly 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00045}.
 REGION      488    547       GoLD.
 COMPBIAS     16     25       Poly-Glu.
 MOD_RES     374    374       Phosphothreonine.
                              {ECO:0000250|UniProtKB:B9EHT4}.
 MOD_RES     401    401       Phosphoserine.
                              {ECO:0000250|UniProtKB:B9EHT4}.
 LIPID       534    534       S-palmitoyl cysteine.
                              {ECO:0000269|PubMed:24001771}.
 LIPID       535    535       S-palmitoyl cysteine.
                              {ECO:0000269|PubMed:24001771}.
 VARIANT     175    175       D -> V (in dbSNP:rs17851002).
                              {ECO:0000269|PubMed:15489334}.
                              /FTId=VAR_027962.
 MUTAGEN     509    509       P->A: Inhibits interaction with ZDHHC13
                              and ZDHHC17.
                              {ECO:0000269|PubMed:26198635}.
 MUTAGEN     534    535       CC->AA: Strongly reduced plasma membrane
                              association and decrease in the levels of
                              Akt at the plasma membrane.
                              {ECO:0000269|PubMed:24001771}.
 HELIX       288    292       {ECO:0000244|PDB:2CP0}.
 STRAND      299    302       {ECO:0000244|PDB:2CP0}.
 TURN        303    305       {ECO:0000244|PDB:2CP0}.
 STRAND      306    314       {ECO:0000244|PDB:2CP0}.
 STRAND      317    319       {ECO:0000244|PDB:2CP0}.
 STRAND      323    331       {ECO:0000244|PDB:2CP0}.
 STRAND      337    339       {ECO:0000244|PDB:2CP0}.
 STRAND      348    350       {ECO:0000244|PDB:2CP0}.
 STRAND      352    355       {ECO:0000244|PDB:2CP0}.
 HELIX       357    359       {ECO:0000244|PDB:2CP0}.
 STRAND      360    362       {ECO:0000244|PDB:2CP0}.
 SEQUENCE   547 AA;  59560 MW;  A718D9673EC1CF4B CRC64;
 MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP LPKDYAFTFF
 DPNDPACQEI LFDPQTTIPE LFAIVRQWVP QVQHKIDVIG NEILRRGCHV NDRDGLTDMT
 LLHYACKAGA HGVGDPAAAV RLSQQLLALG ADVTLRSRWT NMNALHYAAY FDVPDLVRVL
 LKGARPRVVN STCSDFNHGS ALHIAASSLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD
 PMDMSLDKAE AALVAKELRT LLEEAVPLSC ALPKVTLPNY DNVPGNLMLS ALGLRLGDRV
 LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK QGLFASVSKI
 SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKTP SSPSLGSLQQ RDGAKAEVGD
 QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCP PRHGVFAPAS
 RIQRIGGSTD SPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM
 LRAEMQS

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