ID A0A6I8V8E7_DROPS Unreviewed; 1684 AA.
AC A0A6I8V8E7;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE SubName: Full=Restin homolog isoform X3 {ECO:0000313|RefSeq:XP_015035973.2};
GN Name=CLIP-190 {ECO:0000313|RefSeq:XP_015035973.2};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015035973.2};
RN [1] {ECO:0000313|RefSeq:XP_015035973.2}
RP IDENTIFICATION.
RC STRAIN=MV-25-SWS-2005 {ECO:0000313|RefSeq:XP_015035973.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_015035973.2};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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 RefSeq; XP_015035973.2; XM_015180487.2.
DR Proteomes; UP000001819; Chromosome 4.
DR ExpressionAtlas; A0A6I8V8E7; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; Cap-Gly domain; 2.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819}.
FT DOMAIN 222..264
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 338..380
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 555..997
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1023..1510
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1565..1592
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..88
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..162
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1684 AA; 189590 MW; 7B011CDF8F7BBC6D CRC64;
MSDISPDTPA EGAATTPPAE SPAAAPPVEP VATESSDSEL TVVASRIPAP SIRSNIPTPA
SSVTGAAPTS RLKAPSNFGS TSSISSVSKI GRPCCNHTTP KSGPPPRDTN SMSRESDDNL
SSINSAYTDL YQETVKRFTR SSLSPTSDWE RYAASPSPSL SRRSIKSETG SRTSYDHYLE
ATGRRRSSDH NSVVLTANTE QFIIGQKVWV GGLRSGQIAY IGETHFAPGE WAGIVLDEPN
GKNDGYVAGK RYFQCEPKRG IFSRLTRLTV YPMSGALTPT SPLAKNSPER SRTVSPTASI
RSSMMRSPGI GKNGMAVGDR VIVSSGFGSR PGVLRYLGET SFAPGNWCGV ELDEASGKND
GAVDGIRYFE CKPKYGVFVP IAKVSLSPSS KKSRLSRAGS RESLTSIGTM NSIATTNTSR
MRMNAQDLLR EKQQHVEQLM VERELDREDS QNQALQLQRN INELKSRIIQ LESELGDERK
KSEDLQFSID EAQSCGEEYN AQSQVYRKKI HDLESKITKL VSGTSSLQSL APQAAPPTSD
EAEESPLREL ITQLQDKLSA QKQETEARLA EQLEEEQRLR ENLKYLQEQN VILQAELVAK
DESLEKFSLS QSGIDNLRRE LTLLKEENDR QSQEAQALFD QKLAAKAEEL ALVAGQLQQL
KSASDSMMSQ RANMSEECQI LQMEIRMRDE QIKEQRQQVD ELTTQLNVQK ADNSALDDML
RQQQASAEER GVQLQKRLDE LKQIKEAMEK HEQQTQKMEH KLSEVRQLAD QEKLKQEQSL
TAIKQLEQFK SSMEERLAAK LSELEECRRE LIEVQSKLKE TSQLNSEKDF QLSESTETLS
QLRLELEKKS EAYETLLANF ALLRTSHEST VGQNELELQA VQAQLDTKQE ALKTVEDELK
QLQQQVAESD KEGNVQFAKL EEKISELNVQ ARKAAAALAS SQAEVDSKNR QLESTNAALE
KINKDYAESR AEASQLEERL QQISEQLQSE LQAERSSSTD LHMKLTKFSE QMASGQKELT
SKADAWGQEM LQKEREIQDL RQQLHSSQEA LAKLKAESEQ REGALEESIR HLKEELAKIQ
ADQQQLSSGT QETIKELKER LEITNTDLQH KEKMAQEDAQ KISDLKTLVE AIQVANANIS
ETNAELSTVL EVLQAEKSET NHIFELFEME ADMNAERLIE KLTGMKEELK ETHLQQEAAQ
KKCKELELKL QQRNESDQQL HAELLIATEQ MRELEQARIE LQKTIEMKNL HSADLEVKQK
KSDTQLDAQR ISIKELEAKL EEAHEALSKF QADVVKSVMA LQQLQKDNEK LEGSLAKKKE
LVKVLEARLA ETTVQLDTQQ AENKELLQKL EQTQQKEGVL QEATTEQLQQ LKQAKGELQD
ALNKKDNTVK ELGAELKETK SQLDSQRSSL NELQDKLEKA QLKERNVQEE VLKSAEQLRQ
LQQANEELQA SLQQKQGLLE KGNEFDAQLS EYQKVIDEMD DSAKNKFHEV EVLQKRVHEL
EAALHKANEY QKTAILESKQ MSRQLETIER EKTREILALR AQVNGASPRV VVGDQPETEN
SQAKINFLNS IIADMQEKND ELKAKVQALE TQPMDFTKPH AFDIITKRKP APRLFCDICD
EFDKHETEDC PIQASEDRDF SPPPTSETNN NEKKERQLPA PRKYCESCEV FGHDTTECAD
EDTY
//
