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

 CLIP1_RAT               Reviewed;        1320 AA.
Q9JK25; A0A0G2K3T3;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
30-NOV-2016, sequence version 2.
12-SEP-2018, entry version 113.
RecName: Full=CAP-Gly domain-containing linker protein 1;
AltName: Full=Cytoplasmic linker protein 170 {ECO:0000303|PubMed:11290329, ECO:0000303|PubMed:20519438, ECO:0000303|PubMed:26972003};
Short=CLIP-170 {ECO:0000303|PubMed:11290329, ECO:0000303|PubMed:20519438, ECO:0000303|PubMed:26972003};
AltName: Full=Restin;
Name=Clip1; Synonyms=Cyln1, Rsn;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Hippocampus;
PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
Galjart N.;
"Clasps are CLIP-115 and -170 associating proteins involved in the
regional regulation of microtubule dynamics in motile fibroblasts.";
Cell 104:923-935(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
PHOSPHORYLATION AT SER-309; SER-311; SER-314 AND SER-347, MUTAGENESIS
OF SER-309; SER-311; SER-313; SER-319 AND SER-320, AND INTERACTION
WITH DCTN1.
PubMed=20519438; DOI=10.1091/mbc.E09-12-1036;
Lee H.S., Komarova Y.A., Nadezhdina E.S., Anjum R., Peloquin J.G.,
Schober J.M., Danciu O., van Haren J., Galjart N., Gygi S.P.,
Akhmanova A., Borisy G.G.;
"Phosphorylation controls autoinhibition of cytoplasmic linker
protein-170.";
Mol. Biol. Cell 21:2661-2673(2010).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199; SER-203;
SER-309; SER-1116 AND SER-1246, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[5]
PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-309;
SER-311; SER-313; SER-319 AND SER-320, INTERACTION WITH DCTN1, AND
ASSOCIATION WITH MICROTUBULES.
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).
-!- 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 and TUBA1B. Interacts
with SLAIN2. Interacts with MAPRE1 and MAPRE3 (By similarity).
Interacts (via zinc finger) with DCTN1 (PubMed:20519438,
PubMed:26972003). Binds preferentially to tyrosinated
microtubules, and only marginally to detyrosinated microtubules
(PubMed:26972003). {ECO:0000250|UniProtKB:P30622,
ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003}.
-!- INTERACTION:
Q7Z460:CLASP1 (xeno); NbExp=2; IntAct=EBI-908338, EBI-913476;
P67870:CSNK2B (xeno); NbExp=2; IntAct=EBI-908338, EBI-348169;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26972003}. 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:26972003).
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:26972003}.
-!- DOMAIN: Intramolecular interaction between the zinc finger domain
and the CAP-Gly domains may inhibit interaction with tubulin.
{ECO:0000250|UniProtKB:P30622}.
-!- PTM: Phosphorylated. 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 (PubMed:20519438,
PubMed:26972003). Phosphorylation by MTOR may positively regulate
CLIP1 association with microtubules (By similarity).
{ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
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EMBL; AJ237670; CAB92974.1; -; mRNA.
EMBL; AC117299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_113933.2; NM_031745.2.
UniGene; Rn.22069; -.
ProteinModelPortal; Q9JK25; -.
SMR; Q9JK25; -.
IntAct; Q9JK25; 9.
MINT; Q9JK25; -.
iPTMnet; Q9JK25; -.
PhosphoSitePlus; Q9JK25; -.
PRIDE; Q9JK25; -.
Ensembl; ENSRNOT00000078530; ENSRNOP00000072766; ENSRNOG00000001247.
GeneID; 65201; -.
KEGG; rno:65201; -.
UCSC; RGD:67404; rat.
CTD; 6249; -.
RGD; 67404; Clip1.
eggNOG; KOG4568; Eukaryota.
eggNOG; COG5244; LUCA.
GeneTree; ENSGT00760000119173; -.
HOGENOM; HOG000092755; -.
HOVERGEN; HBG007123; -.
KO; K10421; -.
PhylomeDB; Q9JK25; -.
Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-68877; Mitotic Prometaphase.
PRO; PR:Q9JK25; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001247; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
ExpressionAtlas; Q9JK25; baseline and differential.
Genevisible; Q9JK25; RN.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
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;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Membrane; Metal-binding;
Microtubule; Phosphoprotein; Reference proteome; Repeat; Transport;
Zinc; Zinc-finger.
CHAIN 1 1320 CAP-Gly domain-containing linker protein
1.
/FTId=PRO_0000438322.
DOMAIN 78 120 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 231 273 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
ZN_FING 1299 1316 CCHC-type.
{ECO:0000250|UniProtKB:P30622}.
REGION 97 101 Important for tubulin binding.
{ECO:0000250|UniProtKB:P30622}.
COMPBIAS 305 330 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
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:22673903}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:P30622}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:20519438}.
MOD_RES 311 311 Phosphoserine; by PKA.
{ECO:0000269|PubMed:20519438}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000269|PubMed:20519438}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000269|PubMed:20519438}.
MOD_RES 1116 1116 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1246 1246 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 309 309 S->A: Phosphodeficient mutant which
exhibits an open conformation with a high
affinity for microtubules and DCTN1; when
associated with A-311; A-313; A-319 and
A-320. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 309 309 S->E: Phosphomimetic mutant which
exhibits a closed autoinhibited
conformation with a low affinity for
microtubules and DCTN1; when associated
with E-311; E-313; E-319 and E-320.
{ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 311 311 S->A: Phosphodeficient mutant which
exhibits an open conformation with a high
affinity for microtubules and DCTN1; when
associated with A-309; A-313; A-319 and
A-320. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 311 311 S->E: Phosphomimetic mutant which
exhibits a closed autoinhibited
conformation with a low affinity for
microtubules and DCTN1; when associated
with E-309; E-313; E-319 and E-320.
{ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 313 313 S->A: Phosphodeficient mutant which
exhibits an open conformation with a high
affinity for microtubules and DCTN1; when
associated with A-309; A-311; A-319 and
A-320. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 313 313 S->E: Phosphomimetic mutant which
exhibits a closed autoinhibited
conformation with a low affinity for
microtubules and DCTN1; when associated
with E-309; E-311; E-319 and E-320.
{ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 319 319 S->A: Phosphodeficient mutant which
exhibits an open conformation with a high
affinity for microtubules and DCTN1; when
associated with A-309; A-311; A-313 and
A-320. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 319 319 S->E: Phosphomimetic mutant which
exhibits a closed autoinhibited
conformation with a low affinity for
microtubules and DCTN1; when associated
with E-30; E-311; E-313 and E-320.
{ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 320 320 S->A: Phosphodeficient mutant which
exhibits an open conformation with a high
affinity for microtubules and DCTN1; when
associated with A-309; A-311; A-313 and
A-319. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
MUTAGEN 320 320 S->E: Phosphomimetic mutant, exhibits a
closed autoinhibited conformation with a
low affinity for microtubules and DCTN1;
when associated with E-309; E-311; E-313
and E-319. {ECO:0000269|PubMed:20519438,
ECO:0000269|PubMed:26972003}.
CONFLICT 1232 1232 A -> G (in Ref. 1; CAB92974).
SEQUENCE 1320 AA; 148279 MW; 81D8096405D4689D CRC64;
MSMLKPSGLK APTKILKPGS TALKTPAAAA APLEKTVPSE KASGPPSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
PSKLTRKVQA EDEANGLQTA HARAASPLST AAATMVSSSP ATPSNIPQKP SQPVAKETSA
TPQISNLTKT ASESISNLSE AGSVKKGERE LKIGDRVLVG GTKAGVVRFL GETDFAKGEW
CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
TTPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLETQTKL EHARIKELEQ SLLFEKTKAD
KLQRELEDTR VATVSEKSRI MELEKDLALR VQEVAELRRR LESSKPPGDV DMSLSLLQEI
SALQEKLEVT HTDHQNEVTS LKDHFGTREE MFQKEIKALH AATEKLSKEN ESLRSKLDHA
NKENSDVIAL WKSKLETAIA SHQQAMEELK VSFSKGIGTD SAEFAELKTQ IERLRLDYQH
EIESLQSKQD SERSAHAKEM ESMKAKLMKI IKEKEDSLEA VKARLDTAED QHLVEMEEML
SKLQEAEIKK EKFASASEEA VSTQTSMQDT VNKLHQKEEQ FNMLSSELEK LRENLTDMEA
KFKEKDERED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM NDELRLKERS VEELQLKLTK
ANENASLLQK SIGEVTLKAE QSQQEAAKKH EEEKKELENK LLELEKKMET SHYQCQDLKA
KYEKASSETK IKHEEILQNF QKMLVDTEDK LKAAQEANRD LMQDMEELKS QADKAKAAQT
AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA KLQSELDTLK ENNLKTVEEL NKSKELLNEE
NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG RTRDEVTSHQ KLEEERSVLN
NQLLEMKKSL PSNTLRESEY RKDADEEKAS LQKSISLTSA LLTEKDAELE KLRNEVTVLR
GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ LSSSSGNTDV QTEEDERAQE
SQQMIDFLNS VIVDLQRKNQ DLKMKVEMMS EAALNGNGED PNSYDSDDQE KQSKKKPRLF
CDICDCFDLH DTEDCPTQAQ MSEDPPHSTH HGSRSEERPY CEICEMFGHW ATNCNDDETF


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CLC CLASP1 Gene cytoplasmic linker associated protein 1


 

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