Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00190
Entry Name
UniProt Accession
Theoretical PI
8.17
Molecular Weight
59586.94
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
CAP-Gly domain-containing linker protein 3
Protein Synonyms/Alias
Cytoplasmic linker protein 170-related 59 kDa protein; CLIP-170-related 59 kDa protein; CLIPR-59;
Gene Name
Clip3
Gene Synonyms/Alias
Clipr59;
Created Date
22-FEB-2012
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
534
Canonical
SISRLLFCCWFPWML
[1]
S-Palmitoylation
535
Canonical
ISRLLFCCWFPWMLR
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Lallemand-Breitenbach V, Quesnoit M, Braun V, El Marjou A, Poüs C, Goud B,Perez F. CLIPR-59 is a lipid raft-associated protein containing acytoskeleton-associated protein glycine-rich domain (CAP-Gly) that perturbsmicrotubule dynamics. J Biol Chem. 2004 Sep 24;279(39):41168-78. Epub 2004 Jul19.[PMID:15262990]
Functional Description
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 (By similarity).
Sequence Annotation
Domain: 314 356 CAP-Gly 1.
Domain: 436 478 CAP-Gly 2.
Region: 488 547 GoLD.
Protein Length
547 AA.
Protein Sequence
(Canonical)
MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP LPKDYAFTFF  60
DPNDPACQEI LFDPKTTIPE LFAIVRQWVP QVQHKIDVIG NEILRRGCHV NDRDGLTDMT  120
LLHYACKAGA HGVGDPAAAV RLSQQLLALG ADVTLRSRWT NMNALHYAAY FDVPDLVRVL  180
LKGARPRVVN STCSDFNHGS ALHIAASNLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD  240
PMDMSLDKAE AALVAKELRT LLEEAVPLSC TLPKVTLPNY DNVPGNLMLS ALGLRLGDRV  300
LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK QGLFASVSKV  360
SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKSP SSPSLGSLQQ REGAKAEVGD  420
QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCA PRHGVFAPAS  480
RIQRIGGSTD PPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM  540
LRAEMQS                                                            547
FASTA
(Canonical)
>LipidDB-10090-00190|B9EHT4
MTKTDPAPMAPPPRGEEEEEEEEDEPVPEAPSPTQERRQKPVVHPSAPAPLPKDYAFTFF
DPNDPACQEILFDPKTTIPELFAIVRQWVPQVQHKIDVIGNEILRRGCHVNDRDGLTDMT
LLHYACKAGAHGVGDPAAAVRLSQQLLALGADVTLRSRWTNMNALHYAAYFDVPDLVRVL
LKGARPRVVNSTCSDFNHGSALHIAASNLCLGAAKCLLEHGANPALRNRKGQVPAEVVPD
PMDMSLDKAEAALVAKELRTLLEEAVPLSCTLPKVTLPNYDNVPGNLMLSALGLRLGDRV
LLDGQKTGTLRFCGTTEFASGQWVGVELDEPEGKNDGSVGGVRYFICPPKQGLFASVSKV
SKAVDAPPSSVTSTPRTPRMDFSRVTGKGRREHKGKKKSPSSPSLGSLQQREGAKAEVGD
QVLVAGQKQGIVRFYGKTDFAPGYWYGIELDQPTGKHDGSVFGVRYFTCAPRHGVFAPAS
RIQRIGGSTDPPGDSVGAKKVHQVTMTQPKRTFTTVRTPKDIASENSISRLLFCCWFPWM
LRAEMQS
Gene Ontology
GO:0031901; C:early endosome membrane; ISS:UniProtKB
GO:0045121; C:membrane raft; ISS:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0055038; C:recycling endosome membrane; ISS:UniProtKB
GO:0005802; C:trans-Golgi network; IDA:UniProtKB
GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB
GO:0035594; F:ganglioside binding; ISS:UniProtKB
GO:0008017; F:microtubule binding; ISS:UniProtKB
GO:0072321; P:chaperone-mediated protein transport; ISS:UniProtKB
GO:0045444; P:fat cell differentiation; IEP:UniProtKB
GO:0044091; P:membrane biogenesis; ISS:UniProtKB
GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB
GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB
GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB
GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB
GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IDA:UniProtKB
GO:0010828; P:positive regulation of glucose transport; IMP:UniProtKB
GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB
Interpro
InterPro; IPR002110; Ankyrin_rpt
InterPro; IPR020683; Ankyrin_rpt-contain_dom
InterPro; IPR000938; CAP-Gly_domain
Pfam
Pfam; PF12796; Ank_2;
Pfam; PF01302; CAP_GLY;
SMART
SMART; SM00248; ANK;
SMART; SM01052; CAP_GLY;
PROSITE
PROSITE; PS50297; ANK_REP_REGION;
PROSITE; PS50088; ANK_REPEAT;
PROSITE; PS00845; CAP_GLY_1;
PROSITE; PS50245; CAP_GLY_2;
PRINTS