CLIP3_MOUSE
ID CLIP3_MOUSE Reviewed; 547 AA.
AC B9EHT4; Q7TNI1; Q9DB67;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=CAP-Gly domain-containing linker protein 3;
DE AltName: Full=Cytoplasmic linker protein 170-related 59 kDa protein;
DE Short=CLIP-170-related 59 kDa protein;
DE Short=CLIPR-59;
GN Name=Clip3; Synonyms=Clipr59;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-547.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374; SER-399 AND SER-401, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [7]
RP STRUCTURE BY NMR OF 398-486.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 2nd CAP-Gly domain in mouse CLIP170-related
RT 59kDA protein CLIPR-59.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Functions as a cytoplasmic linker protein. Involved in TGN-
CC endosome dynamics. May modulate the cellular compartmentalization of
CC AKT kinase family and promote its cell membrane localization, thereby
CC playing a role in glucose transport in adipocytes (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with AKT1 and AKT2; when AKT1 and AKT2
CC are phosphorylated and activated, affinity is higher for AKT2 (By
CC similarity). Interacts with ZDHHC13 (via ANK repeats)
CC (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
CC (PubMed:26198635). {ECO:0000250|UniProtKB:Q96DZ5,
CC ECO:0000269|PubMed:26198635}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus, Golgi stack
CC {ECO:0000250}. Note=Localized to Golgi stacks as well as on
CC tubulovesicular elements juxtaposed to Golgi cisternae. {ECO:0000250}.
CC -!- DOMAIN: Microtubule association is inhibited by the ANK repeats and the
CC Golgi localization region (GoLD). {ECO:0000250}.
CC -!- PTM: Palmitoylation by ZDHHC17 regulates association with the plasma
CC membrane. {ECO:0000250}.
CC -!- MISCELLANEOUS: The N-terminal half is dispensable for proper Golgi
CC targeting, whereas the GoLD region is required. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23857.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC149067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466593; EDL24034.1; -; Genomic_DNA.
DR EMBL; BC056173; AAH56173.1; -; mRNA.
DR EMBL; BC138413; AAI38414.1; -; mRNA.
DR EMBL; AK005167; BAB23857.1; ALT_INIT; mRNA.
DR CCDS; CCDS39880.1; -.
DR RefSeq; NP_001074583.1; NM_001081114.1.
DR RefSeq; XP_006540473.1; XM_006540410.3.
DR RefSeq; XP_006540474.1; XM_006540411.3.
DR PDB; 1WHH; NMR; -; A=398-486.
DR PDBsum; 1WHH; -.
DR AlphaFoldDB; B9EHT4; -.
DR SMR; B9EHT4; -.
DR BioGRID; 218260; 3.
DR STRING; 10090.ENSMUSP00000014065; -.
DR iPTMnet; B9EHT4; -.
DR PhosphoSitePlus; B9EHT4; -.
DR SwissPalm; B9EHT4; -.
DR MaxQB; B9EHT4; -.
DR PaxDb; B9EHT4; -.
DR PeptideAtlas; B9EHT4; -.
DR PRIDE; B9EHT4; -.
DR ProteomicsDB; 283302; -.
DR Antibodypedia; 48030; 133 antibodies from 23 providers.
DR Ensembl; ENSMUST00000014065; ENSMUSP00000014065; ENSMUSG00000013921.
DR GeneID; 76686; -.
DR KEGG; mmu:76686; -.
DR UCSC; uc009gea.1; mouse.
DR CTD; 25999; -.
DR MGI; MGI:1923936; Clip3.
DR VEuPathDB; HostDB:ENSMUSG00000013921; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000159557; -.
DR HOGENOM; CLU_023687_2_1_1; -.
DR InParanoid; B9EHT4; -.
DR OMA; IELDHPT; -.
DR OrthoDB; 482616at2759; -.
DR PhylomeDB; B9EHT4; -.
DR TreeFam; TF326096; -.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR BioGRID-ORCS; 76686; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Clip3; mouse.
DR PRO; PR:B9EHT4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; B9EHT4; protein.
DR Bgee; ENSMUSG00000013921; Expressed in embryonic brain and 219 other tissues.
DR ExpressionAtlas; B9EHT4; baseline and differential.
DR Genevisible; B9EHT4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0035594; F:ganglioside binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
DR GO; GO:0044091; P:membrane biogenesis; ISS:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0098840; P:protein transport along microtubule; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR030504; CLIP3.
DR PANTHER; PTHR18916:SF77; PTHR18916:SF77; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell membrane; Cytoplasm; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..547
FT /note="CAP-Gly domain-containing linker protein 3"
FT /id="PRO_0000415670"
FT REPEAT 117..158
FT /note="ANK 1"
FT REPEAT 160..191
FT /note="ANK 2"
FT REPEAT 197..229
FT /note="ANK 3"
FT DOMAIN 314..356
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 436..478
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..547
FT /note="GoLD"
FT COMPBIAS 15..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 534
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 535
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1WHH"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 428..437
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 439..449
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:1WHH"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:1WHH"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:1WHH"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:1WHH"
SQ SEQUENCE 547 AA; 59587 MW; 851B8B94DA20A1AD CRC64;
MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP LPKDYAFTFF
DPNDPACQEI LFDPKTTIPE LFAIVRQWVP QVQHKIDVIG NEILRRGCHV NDRDGLTDMT
LLHYACKAGA HGVGDPAAAV RLSQQLLALG ADVTLRSRWT NMNALHYAAY FDVPDLVRVL
LKGARPRVVN STCSDFNHGS ALHIAASNLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD
PMDMSLDKAE AALVAKELRT LLEEAVPLSC TLPKVTLPNY DNVPGNLMLS ALGLRLGDRV
LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK QGLFASVSKV
SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKSP SSPSLGSLQQ REGAKAEVGD
QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCA PRHGVFAPAS
RIQRIGGSTD PPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM
LRAEMQS
