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Protein

CAP-Gly domain-containing linker protein 3

Gene

Clip3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
CAP-Gly domain-containing linker protein 3
Alternative name(s):
Cytoplasmic linker protein 170-related 59 kDa protein
Short name:
CLIP-170-related 59 kDa protein
Short name:
CLIPR-59
Gene namesi
Name:Clip3
Synonyms:Clipr59
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1923936. Clip3.

Subcellular locationi

GO - Cellular componenti

  • early endosome membrane Source: UniProtKB
  • Golgi stack Source: UniProtKB-SubCell
  • membrane raft Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • recycling endosome membrane Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
  • trans-Golgi network membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547CAP-Gly domain-containing linker protein 3PRO_0000415670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei374 – 3741PhosphothreonineCombined sources
Modified residuei399 – 3991PhosphoserineCombined sources
Modified residuei401 – 4011PhosphoserineCombined sources
Lipidationi534 – 5341S-palmitoyl cysteineBy similarity
Lipidationi535 – 5351S-palmitoyl cysteineBy similarity

Post-translational modificationi

Palmitoylation by ZDHHC17 regulates association with the plasma membrane.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiB9EHT4.
PaxDbiB9EHT4.
PeptideAtlasiB9EHT4.
PRIDEiB9EHT4.

PTM databases

iPTMnetiB9EHT4.

Expressioni

Gene expression databases

BgeeiB9EHT4.
ExpressionAtlasiB9EHT4. baseline and differential.
GenevisibleiB9EHT4. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with AKT1 and AKT2; when AKT1 and AKT2 are phosphorylated and activated, affinity is higher for AKT2 (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi218260. 2 interactions.
STRINGi10090.ENSMUSP00000014065.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi406 – 4094Combined sources
Beta strandi420 – 4245Combined sources
Turni425 – 4273Combined sources
Beta strandi428 – 43710Combined sources
Beta strandi439 – 44911Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi456 – 4616Combined sources
Turni471 – 4733Combined sources
Beta strandi474 – 4774Combined sources
Helixi479 – 4813Combined sources
Beta strandi482 – 4843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHHNMR-A399-486[»]
ProteinModelPortaliB9EHT4.
SMRiB9EHT4. Positions 94-241, 286-370, 409-486.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati117 – 15842ANK 1Add
BLAST
Repeati160 – 19132ANK 2Add
BLAST
Repeati197 – 22933ANK 3Add
BLAST
Domaini314 – 35643CAP-Gly 1PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 47843CAP-Gly 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni488 – 54760GoLDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 2510Poly-Glu

Domaini

Microtubule association is inhibited by the ANK repeats and the Golgi localization region (GoLD).By similarity

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 2 CAP-Gly domains.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000007206.
HOVERGENiHBG057079.
InParanoidiB9EHT4.
KOiK10423.
OMAiDNVGAKK.
OrthoDBiEOG75QR3B.
PhylomeDBiB9EHT4.
TreeFamiTF326096.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.30.30.190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000938. CAP-Gly_domain.
IPR030504. CLIP3.
[Graphical view]
PANTHERiPTHR18916:SF11. PTHR18916:SF11. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM01052. CAP_GLY. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF74924. SSF74924. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9EHT4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP
60 70 80 90 100
LPKDYAFTFF DPNDPACQEI LFDPKTTIPE LFAIVRQWVP QVQHKIDVIG
110 120 130 140 150
NEILRRGCHV NDRDGLTDMT LLHYACKAGA HGVGDPAAAV RLSQQLLALG
160 170 180 190 200
ADVTLRSRWT NMNALHYAAY FDVPDLVRVL LKGARPRVVN STCSDFNHGS
210 220 230 240 250
ALHIAASNLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD PMDMSLDKAE
260 270 280 290 300
AALVAKELRT LLEEAVPLSC TLPKVTLPNY DNVPGNLMLS ALGLRLGDRV
310 320 330 340 350
LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK
360 370 380 390 400
QGLFASVSKV SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKSP
410 420 430 440 450
SSPSLGSLQQ REGAKAEVGD QVLVAGQKQG IVRFYGKTDF APGYWYGIEL
460 470 480 490 500
DQPTGKHDGS VFGVRYFTCA PRHGVFAPAS RIQRIGGSTD PPGDSVGAKK
510 520 530 540
VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM LRAEMQS
Length:547
Mass (Da):59,587
Last modified:March 24, 2009 - v1
Checksum:i851B8B94DA20A1AD
GO

Sequence cautioni

The sequence BAB23857.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC149067 Genomic DNA. No translation available.
CH466593 Genomic DNA. Translation: EDL24034.1.
BC056173 mRNA. Translation: AAH56173.1.
BC138413 mRNA. Translation: AAI38414.1.
AK005167 mRNA. Translation: BAB23857.1. Different initiation.
CCDSiCCDS39880.1.
RefSeqiNP_001074583.1. NM_001081114.1.
XP_006540473.1. XM_006540410.2.
XP_006540474.1. XM_006540411.2.
UniGeneiMm.159258.

Genome annotation databases

EnsembliENSMUST00000014065; ENSMUSP00000014065; ENSMUSG00000013921.
GeneIDi76686.
KEGGimmu:76686.
UCSCiuc009gea.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC149067 Genomic DNA. No translation available.
CH466593 Genomic DNA. Translation: EDL24034.1.
BC056173 mRNA. Translation: AAH56173.1.
BC138413 mRNA. Translation: AAI38414.1.
AK005167 mRNA. Translation: BAB23857.1. Different initiation.
CCDSiCCDS39880.1.
RefSeqiNP_001074583.1. NM_001081114.1.
XP_006540473.1. XM_006540410.2.
XP_006540474.1. XM_006540411.2.
UniGeneiMm.159258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHHNMR-A399-486[»]
ProteinModelPortaliB9EHT4.
SMRiB9EHT4. Positions 94-241, 286-370, 409-486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218260. 2 interactions.
STRINGi10090.ENSMUSP00000014065.

PTM databases

iPTMnetiB9EHT4.

Proteomic databases

MaxQBiB9EHT4.
PaxDbiB9EHT4.
PeptideAtlasiB9EHT4.
PRIDEiB9EHT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014065; ENSMUSP00000014065; ENSMUSG00000013921.
GeneIDi76686.
KEGGimmu:76686.
UCSCiuc009gea.1. mouse.

Organism-specific databases

CTDi25999.
MGIiMGI:1923936. Clip3.

Phylogenomic databases

eggNOGiKOG4568. Eukaryota.
COG5244. LUCA.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000007206.
HOVERGENiHBG057079.
InParanoidiB9EHT4.
KOiK10423.
OMAiDNVGAKK.
OrthoDBiEOG75QR3B.
PhylomeDBiB9EHT4.
TreeFamiTF326096.

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.

Miscellaneous databases

ChiTaRSiClip3. mouse.
PROiB9EHT4.
SOURCEiSearch...

Gene expression databases

BgeeiB9EHT4.
ExpressionAtlasiB9EHT4. baseline and differential.
GenevisibleiB9EHT4. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.30.30.190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000938. CAP-Gly_domain.
IPR030504. CLIP3.
[Graphical view]
PANTHERiPTHR18916:SF11. PTHR18916:SF11. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF01302. CAP_GLY. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
SM01052. CAP_GLY. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF74924. SSF74924. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
PS00845. CAP_GLY_1. 2 hits.
PS50245. CAP_GLY_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-547.
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374; SER-399 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  6. "Identification of a novel sequence motif recognized by the ankyrin repeat domain of zDHHC17/13 S-acyltransferases."
    Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.
    J. Biol. Chem. 290:21939-21950(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZDHHC17 AND ZDHHC13.
  7. "Solution structure of the 2nd CAP-Gly domain in mouse CLIP170-related 59kDA protein CLIPR-59."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 398-486.

Entry informationi

Entry nameiCLIP3_MOUSE
AccessioniPrimary (citable) accession number: B9EHT4
Secondary accession number(s): Q7TNI1, Q9DB67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 24, 2009
Last modified: July 6, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The N-terminal half is dispensable for proper Golgi targeting, whereas the GoLD region is required.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.