CLIP1_MOUSE
ID CLIP1_MOUSE Reviewed; 1391 AA.
AC Q922J3; Q571L7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=CAP-Gly domain-containing linker protein 1;
DE AltName: Full=Cytoplasmic linker protein 170 {ECO:0000303|PubMed:26972003};
DE Short=CLIP-170 {ECO:0000303|PubMed:26972003};
DE AltName: Full=Restin;
GN Name=Clip1; Synonyms=Kiaa4046, Rsn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
RX PubMed=16954346; DOI=10.1083/jcb.200512058;
RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
RA Andrieux A., Job D.;
RT "Tubulin tyrosination is a major factor affecting the recruitment of CAP-
RT Gly proteins at microtubule plus ends.";
RL J. Cell Biol. 174:839-849(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
RA Wu X., Kodama A., Fuchs E.;
RT "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has
RT ATPase activity.";
RL Cell 135:137-148(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199; SER-203;
RP SER-314 AND SER-1317, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
RA Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
RT "Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
RT initiation of dynein-driven transport in neurons.";
RL Cell Rep. 14:2637-2652(2016).
RN [10]
RP STRUCTURE BY NMR OF 58-128.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 1st CAP-Gly domain in mouse CLIP-170/Restin.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes microtubule growth
CC and microtubule bundling. Links cytoplasmic vesicles to microtubules
CC and thereby plays an important role in intracellular vesicle
CC trafficking. Plays a role macropinocytosis and endosome trafficking.
CC {ECO:0000250|UniProtKB:P30622}.
CC -!- SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1.
CC Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2.
CC Interacts with TUBA1B, MAPRE1 and MAPRE3. Interacts (via zinc finger)
CC with DCTN1 (By similarity). Binds preferentially to tyrosinated
CC microtubules, and only marginally to detyrosinated microtubules
CC (PubMed:16954346). {ECO:0000250|UniProtKB:P30622,
CC ECO:0000269|PubMed:16954346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection,
CC ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule
CC plus ends. Localizes preferentially to the ends of tyrosinated
CC microtubules (PubMed:16954346). Accumulates in plasma membrane regions
CC with ruffling and protrusions. Associates with the membranes of
CC intermediate macropinocytic vesicles (By similarity).
CC {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q922J3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922J3-2; Sequence=VSP_019425;
CC -!- DOMAIN: Intramolecular interaction between the zinc finger domain and
CC the CAP-Gly domains may inhibit interaction with tubulin.
CC {ECO:0000250|UniProtKB:P30622}.
CC -!- PTM: Phosphorylated (PubMed:26972003). Phosphorylation induces
CC conformational changes by increasing the affinity of the N-terminus for
CC C-terminus, resulting in inhibition of its function thus decreasing its
CC binding to microtubules and DCTN1. Exhibits a folded, autoinhibited
CC conformation when phosphorylated and an open conformation when
CC dephosphorylated with increased binding affinity to microtubules and
CC DCTN1. Phosphorylation regulates its recruitment to tyrosinated
CC microtubules and the recruitment of vesicular cargo to microtubules in
CC neurons. Phosphorylation by MTOR may positively regulate CLIP1
CC association with microtubules (By similarity).
CC {ECO:0000250|UniProtKB:P30622, ECO:0000250|UniProtKB:Q9JK25,
CC ECO:0000269|PubMed:26972003}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK220172; BAD90357.1; ALT_INIT; mRNA.
DR EMBL; BC007191; AAH07191.1; -; mRNA.
DR CCDS; CCDS19667.1; -. [Q922J3-1]
DR CCDS; CCDS71663.1; -. [Q922J3-2]
DR RefSeq; NP_001278158.1; NM_001291229.1. [Q922J3-2]
DR RefSeq; NP_062739.2; NM_019765.5. [Q922J3-1]
DR PDB; 2CP7; NMR; -; A=58-128.
DR PDBsum; 2CP7; -.
DR AlphaFoldDB; Q922J3; -.
DR SMR; Q922J3; -.
DR BioGRID; 207974; 18.
DR IntAct; Q922J3; 5.
DR MINT; Q922J3; -.
DR STRING; 10090.ENSMUSP00000107192; -.
DR iPTMnet; Q922J3; -.
DR PhosphoSitePlus; Q922J3; -.
DR EPD; Q922J3; -.
DR jPOST; Q922J3; -.
DR MaxQB; Q922J3; -.
DR PaxDb; Q922J3; -.
DR PeptideAtlas; Q922J3; -.
DR PRIDE; Q922J3; -.
DR ProteomicsDB; 281684; -. [Q922J3-1]
DR ProteomicsDB; 281685; -. [Q922J3-2]
DR Antibodypedia; 3829; 320 antibodies from 41 providers.
DR DNASU; 56430; -.
DR Ensembl; ENSMUST00000111564; ENSMUSP00000107190; ENSMUSG00000049550. [Q922J3-2]
DR Ensembl; ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550. [Q922J3-1]
DR GeneID; 56430; -.
DR KEGG; mmu:56430; -.
DR UCSC; uc008zoa.2; mouse. [Q922J3-1]
DR UCSC; uc008zob.2; mouse. [Q922J3-2]
DR CTD; 6249; -.
DR MGI; MGI:1928401; Clip1.
DR VEuPathDB; HostDB:ENSMUSG00000049550; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR InParanoid; Q922J3; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; Q922J3; -.
DR TreeFam; TF326096; -.
DR BioGRID-ORCS; 56430; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Clip1; mouse.
DR EvolutionaryTrace; Q922J3; -.
DR PRO; PR:Q922J3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q922J3; protein.
DR Bgee; ENSMUSG00000049550; Expressed in vastus lateralis and 256 other tissues.
DR ExpressionAtlas; Q922J3; baseline and differential.
DR Genevisible; Q922J3; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044354; C:macropinosome; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; IMP:MGI.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Membrane; Metal-binding;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..1391
FT /note="CAP-Gly domain-containing linker protein 1"
FT /id="PRO_0000240672"
FT DOMAIN 78..120
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 231..273
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT ZN_FING 1370..1387
FT /note="CCHC-type"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..101
FT /note="Important for tubulin binding"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT REGION 129..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..1306
FT /evidence="ECO:0000255"
FT COMPBIAS 142..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 311
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JK25"
FT MOD_RES 1317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 695..770
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019425"
FT CONFLICT 47
FT /note="S -> F (in Ref. 1; BAD90357)"
FT /evidence="ECO:0000305"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2CP7"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:2CP7"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2CP7"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:2CP7"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2CP7"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2CP7"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2CP7"
SQ 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
