SCRIB_DANRE
ID SCRIB_DANRE Reviewed; 1724 AA.
AC Q4H4B6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein scribble homolog;
DE AltName: Full=Scribble1;
GN Name=scrib; Synonyms=llk, scrb1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15829519; DOI=10.1242/dev.01810;
RA Wada H., Iwasaki M., Sato T., Masai I., Nishiwaki Y., Tanaka H., Sato A.,
RA Nojima Y., Okamoto H.;
RT "Dual roles of zygotic and maternal Scribble1 in neural migration and
RT convergent extension movements in zebrafish embryos.";
RL Development 132:2273-2285(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1609, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: Scaffold protein involved in different aspects of polarized
CC cells differentiation regulating epithelial and neuronal morphogenesis.
CC Regulates the caudal migration of the nVII motor neurons. Required for
CC convergent extension movements during gastrulation.
CC {ECO:0000269|PubMed:15829519}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15829519};
CC Peripheral membrane protein {ECO:0000269|PubMed:15829519}. Cell
CC junction {ECO:0000250|UniProtKB:Q14160}. Cell junction, adherens
CC junction {ECO:0000250|UniProtKB:Q14160}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q14160}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14160}. Postsynapse
CC {ECO:0000250|UniProtKB:Q14160}. Presynapse
CC {ECO:0000250|UniProtKB:Q14160}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally during early embryonic
CC stages. Initially expressed throughout the embryo then expression is
CC restricted to the brain region. {ECO:0000269|PubMed:15829519}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q14160}.
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DR EMBL; AB188388; BAE07162.1; -; mRNA.
DR RefSeq; NP_001007176.1; NM_001007175.1.
DR AlphaFoldDB; Q4H4B6; -.
DR SMR; Q4H4B6; -.
DR STRING; 7955.ENSDARP00000068701; -.
DR iPTMnet; Q4H4B6; -.
DR PaxDb; Q4H4B6; -.
DR PRIDE; Q4H4B6; -.
DR Ensembl; ENSDART00000074212; ENSDARP00000068701; ENSDARG00000000861.
DR GeneID; 368473; -.
DR KEGG; dre:368473; -.
DR CTD; 23513; -.
DR ZFIN; ZDB-GENE-030616-572; scrib.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154025; -.
DR InParanoid; Q4H4B6; -.
DR OrthoDB; 284114at2759; -.
DR PhylomeDB; Q4H4B6; -.
DR TreeFam; TF351429; -.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR Reactome; R-DRE-9013409; RHOJ GTPase cycle.
DR Reactome; R-DRE-9696264; RND3 GTPase cycle.
DR Reactome; R-DRE-9696270; RND2 GTPase cycle.
DR PRO; PR:Q4H4B6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000000861; Expressed in muscle tissue and 27 other tissues.
DR ExpressionAtlas; Q4H4B6; baseline.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ZFIN.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:ZFIN.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IGI:ZFIN.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:ZFIN.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0097475; P:motor neuron migration; IGI:ZFIN.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001841; P:neural tube formation; IMP:ZFIN.
DR GO; GO:0048884; P:neuromast development; IMP:ZFIN.
DR GO; GO:0001764; P:neuron migration; IMP:ZFIN.
DR GO; GO:0098968; P:neurotransmitter receptor transport postsynaptic membrane to endosome; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0050918; P:positive chemotaxis; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00595; PDZ; 4.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS51450; LRR; 15.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Leucine-rich repeat; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1724
FT /note="Protein scribble homolog"
FT /id="PRO_0000385516"
FT REPEAT 11..34
FT /note="LRR 1"
FT REPEAT 35..58
FT /note="LRR 2"
FT REPEAT 59..81
FT /note="LRR 3"
FT REPEAT 83..105
FT /note="LRR 4"
FT REPEAT 107..127
FT /note="LRR 5"
FT REPEAT 128..150
FT /note="LRR 6"
FT REPEAT 151..174
FT /note="LRR 7"
FT REPEAT 176..196
FT /note="LRR 8"
FT REPEAT 197..219
FT /note="LRR 9"
FT REPEAT 221..242
FT /note="LRR 10"
FT REPEAT 244..265
FT /note="LRR 11"
FT REPEAT 266..288
FT /note="LRR 12"
FT REPEAT 289..311
FT /note="LRR 13"
FT REPEAT 312..334
FT /note="LRR 14"
FT REPEAT 336..357
FT /note="LRR 15"
FT REPEAT 359..380
FT /note="LRR 16"
FT REPEAT 382..405
FT /note="LRR 17"
FT DOMAIN 731..818
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 867..955
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1005..1094
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1101..1193
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..821
FT /note="Sufficient for targeting to adherens junction"
FT /evidence="ECO:0000250"
FT REGION 451..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1430..1461
FT /evidence="ECO:0000255"
FT COMPBIAS 496..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..599
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1609
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 1724 AA; 189519 MW; 87A3D0C0840E77D6 CRC64;
MLKCIPLWRC NRHVESVDKR HCSLTAVPDE IYRYNRSLEE LLLDANQLRE LPKPFFRLHN
LRKLGLSDNE IQKLPPDVAN FTQLVELDIS RNDISEIPEN IKFCQSLEIA DFSGNPLTRL
PDGFTQLRGL AHLSLNDVSL QSLPNDIGNL SNLVTLELRE NLLKSLPSSL SFLVKLEQLD
LGSNVLEVLP DTLGALPNLR ELWLDRNQLS SLPPELGNLR QLVCLDVSEN RLSELPTEIS
GLIALTDLLL SENLLEILPD SIGSLKKLSI LKVNQNRLVH LTDSIGECEN LTELMLTENL
LQSLPRSLGK LKKLTNLNVD RNRLSSVPAE LGGCVSLNVL SLRDNRLGKL PPELANATEL
HVLDVAGNRL QNLPFALANL NLKAMWLAEN QSQPMLKFQT EDDEQTGEKV LTCYLLPQQP
SSSLENLLER SVDEAWPTDT NLNRVSVIQF RDDSKHEEED DETAADKRGL QRRATPHPSE
LKVMKNVIEA RRNEAYTARP DEDLESPDAE EKRLSGLSNQ SHDSQASSST TSATSHEDKQ
GINSTGVELN DGQVQEEEDL DEMEVEYTEP TVHFAEEPII RGGDEDDDYD NDDDDAERSD
EVSQTPSFPA EKQRLIRKDT PHYKKHFKIT KLPKPETVAA LLQGFSHDGL SPTAHTPENE
RDGEDDEEEE EDEDEEDDLH TPFQHRLDAA ELEDIRMSQM NSSLQPVKGV SFDQVNNLLI
EPARIEEEEL TLSILRQTGG LGISIAGGKG STPYKGDDEG IFISRVSEEG PAARAGVKVG
DKLLEVNGVD LHGAEHHTAV EALRNSGAAV VMTVLRERMV EPENAITTTP LRPEDDYFPR
ERRSSGLPFL LDPDCPAVST GPAQRLATCL IRNDKGLGFS IAGGKGSTLY RVGDTGIFIS
RIAEGGAAHR DNILQVGDRV ISINGVDMTE ARHDQAVALL TGTSPTITLV VDREQSSVGG
ASPRTRPHSP PPPEPSDSPE QEDGGDEHLG NHLNCPMEDE YPIEEVTLIK AGGPLGLSIV
GGSDHASHPF GINEPGVFIS KVIPNGLASQ SGLRVGDRIL EVNSIDLRHA THQEAVRALL
SNKQEIRMLV RRDPSPPGMQ EIVIHKQPGE KLGISIRGGA KGHAGNPFDP TDEGIFISKV
SSNGAAARDG RLRVGMRILE VGNNSLLGMT HTEAVRVLRA SGDSLVMLIC DGFDPKSAST
IEASPGVIAN PFAAGIVRKN SMESISSVDR DLSPEEIDIM QKEVEMVRET SQWEREEMEK
VSLSSGPLKL DYKTLAALPT TSLQKVNRAS PSEPFRIDSP VRDAAHSPHN SQSNIHFPSN
ANTKDNASTK PGAIQPLSRV RPPVSPASQD GHSSPNPFQH GLSPINSQTT DLYSPRNNVS
AKQPSPETPS PLGRHSPEQR SFKDRQKYFE IDVKQQTPDK PKPRISLVGE DDLKKMKEEE
AKRIEQRARE FMLDEDEEEE EEDLAKQVAH MKAHGKVVLD GVEYKVESLG SPTSRQCATP
PNYSATPPSH CGSSGPSSID GKGDSQRNSV EDSFRLEQRP NSMTGLIPVY PGESAAPIRT
AKAERRHQDR LRMQSPELTV ALDKELSPAE KRALEAEKRA MWRAARMKSL EQDALKAQMV
IAKSKEGKKR GTLDQLSESP SPAPTPSPTP MEDISPRTVT SPGRLSPGAA DDVHFMDESS
SNAVSVIDPE VPVAATSALE EMALYSNKRK LRQGRRSLEA PVPT
