CLIP2_MOUSE
ID CLIP2_MOUSE Reviewed; 1047 AA.
AC Q9Z0H8; Q7TSI9; Q8CHU1; Q9EP81;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=CAP-Gly domain-containing linker protein 2;
DE AltName: Full=Cytoplasmic linker protein 115;
DE Short=CLIP-115;
DE AltName: Full=Cytoplasmic linker protein 2;
GN Name=Clip2; Synonyms=Cyln2, Kiaa0291;
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 [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9799601; DOI=10.1006/geno.1998.5529;
RA Hoogenraad C.C., Eussen B.H.J., Langeveld A., van Haperen R.,
RA Winterberg S., Wouters C.H., Grosveld F., de Zeeuw C.I., Galjart N.;
RT "The murine CYLN2 gene: genomic organization, chromosome localization, and
RT comparison to the human gene that is located within the 7q11.23 Williams
RT syndrome critical region.";
RL Genomics 53:348-358(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Green E.D.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 [4]
RP INTERACTION WITH CLASP1 AND CLASP2.
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9427243; DOI=10.1016/s0896-6273(00)80411-0;
RA de Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E., Neubauer A.,
RA Grosveld F.G., Galjart N.J.;
RT "CLIP-115, a novel brain specific cytoplasmic linker protein, mediates the
RT localisation of dendritic lamellar bodies.";
RL Neuron 19:1187-1199(1997).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-208; SER-212;
RP SER-315; SER-974 AND SER-980, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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).
CC -!- FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB),
CC a membranous organelle predominantly present in bulbous dendritic
CC appendages of neurons linked by dendrodendritic gap junctions. May
CC operate in the control of brain-specific organelle translocations (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CLASP1 and CLASP2 (PubMed:11290329). Binds
CC preferentially to tyrosinated microtubules, and only marginally to
CC detyrosinated microtubules (PubMed:16954346).
CC {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:16954346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55156}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Note=Localizes
CC preferentially to the ends of tyrosinated microtubules.
CC {ECO:0000269|PubMed:16954346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0H8-2; Sequence=VSP_015683;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, and very low levels in
CC kidneys. {ECO:0000269|PubMed:9427243}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 10.5 dpc, expression declines until
CC birth after which it suddenly increases. Expression gradually decreases
CC until postnatal day 10, (the day when DLBs start to occur), then again
CC increases and reaches the levels present in adult brain.
CC {ECO:0000269|PubMed:9427243}.
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DR EMBL; AJ228863; CAA13068.1; -; Genomic_DNA.
DR EMBL; AJ228865; CAA13069.1; -; Genomic_DNA.
DR EMBL; AJ228868; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228869; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228870; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228872; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228876; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228880; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228867; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228875; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228871; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228873; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228877; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228866; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228879; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228878; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AJ228874; CAA13069.1; JOINED; Genomic_DNA.
DR EMBL; AF289667; AAF99340.1; -; Genomic_DNA.
DR EMBL; AF289664; AAF99333.1; -; Genomic_DNA.
DR EMBL; BC039162; AAH39162.1; -; mRNA.
DR EMBL; BC053048; AAH53048.1; -; mRNA.
DR CCDS; CCDS39309.1; -. [Q9Z0H8-2]
DR CCDS; CCDS39310.1; -. [Q9Z0H8-1]
DR PIR; T42720; T42720.
DR RefSeq; NP_001034251.1; NM_001039162.2. [Q9Z0H8-2]
DR RefSeq; NP_034120.2; NM_009990.3. [Q9Z0H8-1]
DR AlphaFoldDB; Q9Z0H8; -.
DR SMR; Q9Z0H8; -.
DR BioGRID; 234703; 11.
DR IntAct; Q9Z0H8; 7.
DR MINT; Q9Z0H8; -.
DR STRING; 10090.ENSMUSP00000098212; -.
DR iPTMnet; Q9Z0H8; -.
DR PhosphoSitePlus; Q9Z0H8; -.
DR SwissPalm; Q9Z0H8; -.
DR EPD; Q9Z0H8; -.
DR jPOST; Q9Z0H8; -.
DR MaxQB; Q9Z0H8; -.
DR PaxDb; Q9Z0H8; -.
DR PeptideAtlas; Q9Z0H8; -.
DR PRIDE; Q9Z0H8; -.
DR ProteomicsDB; 279107; -. [Q9Z0H8-1]
DR ProteomicsDB; 279108; -. [Q9Z0H8-2]
DR Antibodypedia; 14611; 168 antibodies from 25 providers.
DR DNASU; 269713; -.
DR Ensembl; ENSMUST00000036999; ENSMUSP00000037431; ENSMUSG00000063146. [Q9Z0H8-2]
DR Ensembl; ENSMUST00000100647; ENSMUSP00000098212; ENSMUSG00000063146. [Q9Z0H8-1]
DR GeneID; 269713; -.
DR KEGG; mmu:269713; -.
DR UCSC; uc008zwi.2; mouse. [Q9Z0H8-1]
DR UCSC; uc008zwj.2; mouse. [Q9Z0H8-2]
DR CTD; 7461; -.
DR MGI; MGI:1313136; Clip2.
DR VEuPathDB; HostDB:ENSMUSG00000063146; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000159426; -.
DR HOGENOM; CLU_001753_0_0_1; -.
DR InParanoid; Q9Z0H8; -.
DR OMA; GTQYFAC; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; Q9Z0H8; -.
DR TreeFam; TF326096; -.
DR BioGRID-ORCS; 269713; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Clip2; mouse.
DR PRO; PR:Q9Z0H8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z0H8; protein.
DR Bgee; ENSMUSG00000063146; Expressed in cortical plate and 125 other tissues.
DR Genevisible; Q9Z0H8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:1901588; C:dendritic microtubule; ISO:MGI.
DR GO; GO:0042599; C:lamellar body; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR028394; CLIP2.
DR PANTHER; PTHR18916:SF10; PTHR18916:SF10; 1.
DR Pfam; PF01302; CAP_GLY; 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 Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1047
FT /note="CAP-Gly domain-containing linker protein 2"
FT /id="PRO_0000083516"
FT DOMAIN 100..142
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 240..282
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..525
FT /evidence="ECO:0000255"
FT COILED 564..637
FT /evidence="ECO:0000255"
FT COILED 677..1017
FT /evidence="ECO:0000255"
FT COMPBIAS 22..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55156"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UDT6"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 462..496
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015683"
FT CONFLICT 25
FT /note="V -> I (in Ref. 3; AAH39162)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> A (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="D -> H (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="G -> A (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 334..335
FT /note="RP -> PA (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="T -> I (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="R -> D (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 713..719
FT /note="SQHRLEL -> AASAEA (in Ref. 1; CAA13068)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="A -> V (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="A -> V (in Ref. 1; CAA13068/CAA13069)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="N -> D (in Ref. 3; AAH39162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 115910 MW; 8F46948122F58872 CRC64;
MQKPSGLKPP GRGGKHSSPV GRPSVGSASS SVVASTSGSK EGSPLHKQAS GPSSSGAATT
VSEKPGPKAA EVGDDFLGDF VVGERVWVNG VKPGVVQYLG ETQFAPGQWA GVVLDDPVGK
NDGAVGGVRY FECPALQGIF TRPSKLTRQP TAEGSGSDTH SVESLTAQNL SLHSGTATPP
LTGRVIPLRE SVLNSSVKTG NESGSNLSDS GSVKRGDKDL HLGDRVLVGG TKTGVVRYVG
ETDFAKGEWC GVELDEPLGK NDGAVAGTRY FQCPPKFGLF APIHKVIRIG FPSTSPAKAK
KTKRMAMGVS ALTHSPSSSS ISSVSSVASS VGGRPSRSGL LTETSSRYAR KISGTTALQE
ALKEKQQHIE QLLAERDLER AEVAKATSHI CEVEKEIALL KAQHEQYVAE AEEKLQRARL
LVENVRKEKV DLSNQLEEER RKVEDLQFRV EEESITKGDL ETQTQLEHAR IGELEQSLLL
EKAQAERLLR ELADNRLTTV AEKSRVLQLE EELSLRRGEI EELQHCLLQS GPPPADHPEA
AETLRLRERL LSASKEHQRD STLLQDKYEH MLKTYQTEVD KLRAANEKYA QEVADLKAKV
QQATTENMGL MDNWKSKLDS LASDHQKSLE DLKATLNSGP GAQQKEIGEL KALVEGIKME
HQLELGNLQA KHDLETAMHG KEKEGLRQKL QEVQEELAGL QQHWREQLEE QASQHRLELQ
EAQDQCRDAQ LRAQELEGLD VEYRGQAQAI EFLKEQISLA EKKMLDYEML QRAEAQSRQE
AERLREKLLV AENRLQAAES LCSAQHSHVI ESSDLSEETI RMKETVEGLQ DKLNKRDKEV
TALTSQMDML RAQVSALENK CKSGEKKIDS LLKEKRRLEA ELEAVSRKTH DASGQLVHIS
QELLRKERSL NELRVLLLEA NRHSPGPERD LSREVHKAEW RIKEQKLKDD IRGLREKLTG
LDKEKSLSEQ RRYSLIDPAS PPELLKLQHQ LVSTEDALRD ALNQAQQVER LVEALRGCSD
RTQTISNSGS ANGIHQPDKA HKQEDKH
