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CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 170) (CLIP-170) (Restin)

 CLIP1_MOUSE             Reviewed;        1391 AA.
Q922J3; Q571L7;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 135.
RecName: Full=CAP-Gly domain-containing linker protein 1;
AltName: Full=Cytoplasmic linker protein 170 {ECO:0000303|PubMed:26972003};
Short=CLIP-170 {ECO:0000303|PubMed:26972003};
AltName: Full=Restin;
Name=Clip1; Synonyms=Kiaa4046, Rsn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryonic tail;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[4]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
PubMed=16954346; DOI=10.1083/jcb.200512058;
Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
Andrieux A., Job D.;
"Tubulin tyrosination is a major factor affecting the recruitment of
CAP-Gly proteins at microtubule plus ends.";
J. Cell Biol. 174:839-849(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-203, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
SUBCELLULAR LOCATION.
PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
Wu X., Kodama A., Fuchs E.;
"ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and
has ATPase activity.";
Cell 135:137-148(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199; SER-203;
SER-314 AND SER-1317, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
PHOSPHORYLATION.
PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
"Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
initiation of dynein-driven transport in neurons.";
Cell Rep. 14:2637-2652(2016).
[10]
STRUCTURE BY NMR OF 58-128.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 1st CAP-Gly domain in mouse CLIP-
170/Restin.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Binds to the plus end of microtubules and regulates the
dynamics of the microtubule cytoskeleton. Promotes microtubule
growth and microtubule bundling. Links cytoplasmic vesicles to
microtubules and thereby plays an important role in intracellular
vesicle trafficking. Plays a role macropinocytosis and endosome
trafficking. {ECO:0000250|UniProtKB:P30622}.
-!- SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1.
Interacts (via CAP-Gly domains) with tubulin. Interacts with
SLAIN2. Interacts with TUBA1B, MAPRE1 and MAPRE3. Interacts (via
zinc finger) with DCTN1 (By similarity). Binds preferentially to
tyrosinated microtubules, and only marginally to detyrosinated
microtubules (PubMed:16954346). {ECO:0000250|UniProtKB:P30622,
ECO:0000269|PubMed:16954346}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasmic
vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Cell projection, ruffle {ECO:0000250|UniProtKB:P30622}.
Note=Localizes to microtubule plus ends. Localizes preferentially
to the ends of tyrosinated microtubules (PubMed:16954346).
Accumulates in plasma membrane regions with ruffling and
protrusions. Associates with the membranes of intermediate
macropinocytic vesicles (By similarity).
{ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q922J3-1; Sequence=Displayed;
Name=2;
IsoId=Q922J3-2; Sequence=VSP_019425;
-!- DOMAIN: Intramolecular interaction between the zinc finger domain
and the CAP-Gly domains may inhibit interaction with tubulin.
{ECO:0000250|UniProtKB:P30622}.
-!- PTM: Phosphorylated (PubMed:26972003). Phosphorylation induces
conformational changes by increasing the affinity of the N-
terminus for C-terminus, resulting in inhibition of its function
thus decreasing its binding to microtubules and DCTN1. Exhibits a
folded, autoinhibited conformation when phosphorylated and an open
conformation when dephosphorylated with increased binding affinity
to microtubules and DCTN1. Phosphorylation regulates its
recruitment to tyrosinated microtubules and the recruitment of
vesicular cargo to microtubules in neurons. Phosphorylation by
MTOR may positively regulate CLIP1 association with microtubules
(By similarity). {ECO:0000250|UniProtKB:P30622,
ECO:0000250|UniProtKB:Q9JK25, ECO:0000269|PubMed:26972003}.
-!- SEQUENCE CAUTION:
Sequence=BAD90357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK220172; BAD90357.1; ALT_INIT; mRNA.
EMBL; BC007191; AAH07191.1; -; mRNA.
CCDS; CCDS19667.1; -. [Q922J3-1]
CCDS; CCDS71663.1; -. [Q922J3-2]
RefSeq; NP_001278158.1; NM_001291229.1. [Q922J3-2]
RefSeq; NP_062739.2; NM_019765.5. [Q922J3-1]
UniGene; Mm.241109; -.
UniGene; Mm.441802; -.
PDB; 2CP7; NMR; -; A=58-128.
PDBsum; 2CP7; -.
ProteinModelPortal; Q922J3; -.
SMR; Q922J3; -.
BioGrid; 207974; 6.
IntAct; Q922J3; 6.
MINT; Q922J3; -.
STRING; 10090.ENSMUSP00000107192; -.
iPTMnet; Q922J3; -.
PhosphoSitePlus; Q922J3; -.
EPD; Q922J3; -.
PaxDb; Q922J3; -.
PeptideAtlas; Q922J3; -.
PRIDE; Q922J3; -.
Ensembl; ENSMUST00000111564; ENSMUSP00000107190; ENSMUSG00000049550. [Q922J3-2]
Ensembl; ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550. [Q922J3-1]
GeneID; 56430; -.
KEGG; mmu:56430; -.
UCSC; uc008zoa.2; mouse. [Q922J3-1]
UCSC; uc008zob.2; mouse. [Q922J3-2]
CTD; 6249; -.
MGI; MGI:1928401; Clip1.
eggNOG; KOG4568; Eukaryota.
eggNOG; COG5244; LUCA.
GeneTree; ENSGT00760000119173; -.
HOGENOM; HOG000092755; -.
HOVERGEN; HBG007123; -.
InParanoid; Q922J3; -.
KO; K10421; -.
PhylomeDB; Q922J3; -.
TreeFam; TF326096; -.
Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-68877; Mitotic Prometaphase.
ChiTaRS; Clip1; mouse.
EvolutionaryTrace; Q922J3; -.
PRO; PR:Q922J3; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000049550; Expressed in 288 organ(s), highest expression level in muscle tissue.
CleanEx; MM_CLIP1; -.
ExpressionAtlas; Q922J3; baseline and differential.
Genevisible; Q922J3; MM.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044354; C:macropinosome; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
GO; GO:0044861; P:protein transport into plasma membrane raft; IMP:MGI.
Gene3D; 2.30.30.190; -; 2.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR032108; CLIP1_ZNF.
Pfam; PF01302; CAP_GLY; 2.
Pfam; PF16641; CLIP1_ZNF; 2.
SMART; SM01052; CAP_GLY; 2.
SUPFAM; SSF74924; SSF74924; 2.
PROSITE; PS00845; CAP_GLY_1; 2.
PROSITE; PS50245; CAP_GLY_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Membrane; Metal-binding; Microtubule; Phosphoprotein;
Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
CHAIN 1 1391 CAP-Gly domain-containing linker protein
1.
/FTId=PRO_0000240672.
DOMAIN 78 120 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 231 273 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
ZN_FING 1370 1387 CCHC-type.
{ECO:0000250|UniProtKB:P30622}.
REGION 97 101 Important for tubulin binding.
{ECO:0000250|UniProtKB:P30622}.
COILED 349 1306 {ECO:0000255}.
COMPBIAS 305 330 Ser-rich.
MOD_RES 48 48 Phosphoserine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 311 311 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 1189 1189 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JK25}.
MOD_RES 1317 1317 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 695 770 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_019425.
CONFLICT 47 47 S -> F (in Ref. 1; BAD90357).
{ECO:0000305}.
STRAND 63 66 {ECO:0000244|PDB:2CP7}.
STRAND 71 79 {ECO:0000244|PDB:2CP7}.
STRAND 81 83 {ECO:0000244|PDB:2CP7}.
STRAND 85 95 {ECO:0000244|PDB:2CP7}.
STRAND 97 103 {ECO:0000244|PDB:2CP7}.
STRAND 116 119 {ECO:0000244|PDB:2CP7}.
HELIX 121 123 {ECO:0000244|PDB:2CP7}.
SEQUENCE 1391 AA; 155814 MW; 061BED1FB3D4068D CRC64;
MSMLKPSGLK APTKILKPGS TALKTPAAAA APVEKTIPSE KASGPPSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
PSKLTRKVQA EDEANGLQAA PGRTASPLST AAATMVSSSP ATPSNIPHKP SQSTAKEPSA
TPQISNLTKT ASESISNLSE AGSVKKGERE LKVGDRVLVG GTKAGVVRFL GETDFAKGEW
CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
ATPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLEVATVS EKSRIMELEK DLALRAQEVA
ELRRRLESSK PPGDVDMSLS LLQEISALQE KLEAIHTDHQ GEMTSLKEHF GAREEAFQKE
IKALHTATEK LSKENESLRS KLDHANKENS DVIALWKSKL ETAIASHQQA MEELKVSFSK
GIGTDSAEFA ELKTQIERLR LDYQHEIESL QSKQDSERSA HAKEMETMQA KLMKIIKEKE
DSLEAVKARL DSAEDQHLVE MEDTLNKLQE AEIKVKELEV LQAKYTEQSE VIGNFTSQLS
AVKEKLLDLD ALRKANSEGK LELETLRQQL EGAEKQIKNL ETERNAESSK ANSITKELQE
KELVLTGLQD SLNQVNQVKE TLEKELQTLK EKFASTSEEA VSAQTRMQDT VNKLHQKEEQ
FNVLSSELEK LRENLTDMEA KFKEKDDRED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM
NDELRLKERS VEELQLKLTK ANENASFLQK SIGEVTLKAE QSQQQAARKH EEEKKELEEK
LLELEKKMET SYNQCQDLKA KYEKASSETK TKHEEILQNL QKMLADTEDK LKAAQEANRD
LMQDMEELKT QADKAKAAQT AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA RLQNELDTLK
ENNLKTVEEL NKSKELLSVE NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG
RTRDEVTSHQ KLEEERSVLN NQLLEMKKRE SEFRKDADEE KASLQKSISL TSALLTEKDA
ELEKLRNEVT VLRGENATAK SLHSVVQTLE SDKVKLELKV KNLELQLKEN KRQLSSSSGN
TDAQAEEDER AQESQIDFLN SVIVDLQRKN QDLKMKVEMM SEAALNGNGE DLNSYDSDDQ
EKQSKKKPRL FCDICDCFDL HDTEDCPTQA QMSEDPPHST HHGSRSEERP YCEICEMFGH
WATNCNDDET F


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