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CAP-Gly domain-containing linker protein 2 (Cytoplasmic linker protein 115) (CLIP-115) (Cytoplasmic linker protein 2)

 CLIP2_RAT               Reviewed;        1046 AA.
O55156;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=CAP-Gly domain-containing linker protein 2;
AltName: Full=Cytoplasmic linker protein 115;
Short=CLIP-115;
AltName: Full=Cytoplasmic linker protein 2;
Name=Clip2; Synonyms=Cyln2;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=9427243; DOI=10.1016/S0896-6273(00)80411-0;
de Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E.,
Neubauer A., Grosveld F.G., Galjart N.J.;
"CLIP-115, a novel brain specific cytoplasmic linker protein, mediates
the localisation of dendritic lamellar bodies.";
Neuron 19:1187-1199(1997).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-208 AND
SER-923, 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).
-!- FUNCTION: Seems to link microtubules to dendritic lamellar body
(DLB), a membranous organelle predominantly present in bulbous
dendritic appendages of neurons linked by dendrodendritic gap
junctions. May operate in the control of brain-specific organelle
translocations. {ECO:0000269|PubMed:9427243}.
-!- SUBUNIT: Interacts with CLASP1 and CLASP2. Binds preferentially to
tyrosinated microtubules, and only marginally to detyrosinated
microtubules. {ECO:0000250|UniProtKB:Q9Z0H8}.
-!- INTERACTION:
Q7Z460:CLASP1 (xeno); NbExp=3; IntAct=EBI-349416, EBI-913476;
Q80TV8:Clasp1 (xeno); NbExp=3; IntAct=EBI-349416, EBI-908322;
O75122:CLASP2 (xeno); NbExp=3; IntAct=EBI-349416, EBI-913524;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9427243}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9427243}.
Note=Localizes preferentially to the ends of tyrosinated
microtubules. {ECO:0000250|UniProtKB:Q9Z0H8}.
-!- TISSUE SPECIFICITY: Brain-specific, expressed in the hippocampus,
inferior olive, and piriform cortex and in the cerebellum (at
protein level). {ECO:0000269|PubMed:9427243}.
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EMBL; AJ000485; CAA04123.1; -; mRNA.
PIR; T42734; T42734.
UniGene; Rn.10893; -.
ProteinModelPortal; O55156; -.
SMR; O55156; -.
BioGrid; 247936; 2.
IntAct; O55156; 4.
STRING; 10116.ENSRNOP00000035734; -.
iPTMnet; O55156; -.
PhosphoSitePlus; O55156; -.
PaxDb; O55156; -.
PRIDE; O55156; -.
UCSC; RGD:62019; rat.
RGD; 62019; Clip2.
eggNOG; KOG4568; Eukaryota.
eggNOG; COG5244; LUCA.
HOGENOM; HOG000092755; -.
HOVERGEN; HBG007123; -.
InParanoid; O55156; -.
PhylomeDB; O55156; -.
PRO; PR:O55156; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; TAS:UniProtKB.
GO; GO:1901588; C:dendritic microtubule; IDA:RGD.
GO; GO:0042599; C:lamellar body; IDA:RGD.
GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; TAS:RGD.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; NAS:UniProtKB.
Gene3D; 2.30.30.190; -; 2.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR028394; CLIP2.
PANTHER; PTHR18916:SF10; PTHR18916:SF10; 1.
Pfam; PF01302; CAP_GLY; 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;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 1046 CAP-Gly domain-containing linker protein
2.
/FTId=PRO_0000083517.
DOMAIN 100 142 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 240 282 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
COILED 355 525 {ECO:0000255}.
COILED 564 637 {ECO:0000255}.
COILED 675 966 {ECO:0000255}.
COILED 994 1014 {ECO:0000255}.
COMPBIAS 315 346 Ser-rich.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0H8}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0H8}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0H8}.
MOD_RES 923 923 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0H8}.
MOD_RES 979 979 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0H8}.
SEQUENCE 1046 AA; 115480 MW; 72E6CE9F76D2A1D0 CRC64;
MQKPSGLKPP GRGGKHSSPV GRPSIGSASS SVVASASGSK EGSPLHKQAS GPSSAGATTT
VSEKPGPKAA EVGDDFLGDF VVGERVWVNG VKPGVVQYLG ETQFAPGQWA GVVLDDPVGK
NDGAVGGLRY FECPALQGIF TRPSKLTRQP AAEGSGSDGH 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 QEAQEELAGL QQHWRAQLEE QAAAPAELQE
AQDQCRDAQL RVQELEGLDV EYRGQAQAIE FLKEQISLAE KKMLDYEMLQ RAEAQSRQEA
ERLREKLLVA ENRLQAVESL CSAQHSHVIE SNDLSEEKIR MKETVEGLQD KLNKRDKEVA
ALTSQMDMLR AQVSALENKC KSGEKKIDSL LKEKRRLEAE LEAVSRKTHD ASGQLVHISQ
ELLRKERSLN ELRVLLLEAN RHSPGPERDL SREVHKAEWR IKEQKLKDDI RGLREKLTGL
DKEKSLSEQK RYSLIDPASA PELLRLQHQL VSTEGCLRDA LDQAQQVERL VEALRGCSDR
TQTISNSGSA NGIHQPDKAH KQEDKH


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