CLIP3_PONAB
ID CLIP3_PONAB Reviewed; 547 AA.
AC Q5R686;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC Interacts with ZDHHC13 (via ANK repeats). Interacts with ZDHHC17 (via
CC ANK repeats). {ECO:0000250|UniProtKB:Q96DZ5}.
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}.
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DR EMBL; CR860608; CAH92730.1; -; mRNA.
DR RefSeq; NP_001126592.1; NM_001133120.1.
DR AlphaFoldDB; Q5R686; -.
DR SMR; Q5R686; -.
DR STRING; 9601.ENSPPYP00000011075; -.
DR GeneID; 100173588; -.
DR KEGG; pon:100173588; -.
DR CTD; 25999; -.
DR eggNOG; KOG4568; Eukaryota.
DR InParanoid; Q5R686; -.
DR OrthoDB; 482616at2759; -.
DR Proteomes; UP000001595; Unplaced.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS: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:0045444; P:fat cell differentiation; ISS: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; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS: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 2: Evidence at transcript level;
KW ANK repeat; Cell membrane; Cytoplasm; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..547
FT /note="CAP-Gly domain-containing linker protein 3"
FT /id="PRO_0000076213"
FT REPEAT 117..155
FT /note="ANK 1"
FT REPEAT 160..189
FT /note="ANK 2"
FT REPEAT 197..226
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:0000250|UniProtKB:B9EHT4"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B9EHT4"
FT LIPID 534
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 535
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 59659 MW; B719D9672EC0C33A 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 RDRAKAEVGD
QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCP PRHGVFAPAS
RIQRIGGSTD SPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM
LRAEMQS
