CLIP2_RAT
ID CLIP2_RAT Reviewed; 1046 AA.
AC O55156;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 129.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-208 AND SER-923, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000269|PubMed:9427243}.
CC -!- SUBUNIT: Interacts with CLASP1 and CLASP2. Binds preferentially to
CC tyrosinated microtubules, and only marginally to detyrosinated
CC microtubules. {ECO:0000250|UniProtKB:Q9Z0H8}.
CC -!- INTERACTION:
CC O55156; Q7Z460: CLASP1; Xeno; NbExp=3; IntAct=EBI-349416, EBI-913476;
CC O55156; Q80TV8: Clasp1; Xeno; NbExp=3; IntAct=EBI-349416, EBI-908322;
CC O55156; O75122: CLASP2; Xeno; NbExp=3; IntAct=EBI-349416, EBI-913524;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9427243}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9427243}. Note=Localizes
CC preferentially to the ends of tyrosinated microtubules.
CC {ECO:0000250|UniProtKB:Q9Z0H8}.
CC -!- TISSUE SPECIFICITY: Brain-specific, expressed in the hippocampus,
CC inferior olive, and piriform cortex and in the cerebellum (at protein
CC level). {ECO:0000269|PubMed:9427243}.
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DR EMBL; AJ000485; CAA04123.1; -; mRNA.
DR PIR; T42734; T42734.
DR AlphaFoldDB; O55156; -.
DR SMR; O55156; -.
DR BioGRID; 247936; 2.
DR IntAct; O55156; 6.
DR STRING; 10116.ENSRNOP00000035734; -.
DR iPTMnet; O55156; -.
DR PhosphoSitePlus; O55156; -.
DR jPOST; O55156; -.
DR PaxDb; O55156; -.
DR PRIDE; O55156; -.
DR UCSC; RGD:62019; rat.
DR RGD; 62019; Clip2.
DR eggNOG; KOG4568; Eukaryota.
DR InParanoid; O55156; -.
DR PhylomeDB; O55156; -.
DR PRO; PR:O55156; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; TAS:UniProtKB.
DR GO; GO:1901588; C:dendritic microtubule; IDA:RGD.
DR GO; GO:0042599; C:lamellar body; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; NAS:UniProtKB.
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 Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1046
FT /note="CAP-Gly domain-containing linker protein 2"
FT /id="PRO_0000083517"
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..72
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 1021..1046
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 675..966
FT /evidence="ECO:0000255"
FT COILED 994..1014
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:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0H8"
SQ 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
