CIP1_ARATH
ID CIP1_ARATH Reviewed; 1586 AA.
AC F4JZY1; Q38843; Q9FJ35;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=COP1-interactive protein 1 {ECO:0000303|PubMed:7753789};
GN Name=CIP1 {ECO:0000303|PubMed:7753789};
GN OrderedLocusNames=At5g41790 {ECO:0000312|Araport:AT5G41790};
GN ORFNames=K16L22.7 {ECO:0000312|EMBL:BAB10654.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 250-748, INTERACTION WITH COP1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=7753789; DOI=10.1073/pnas.92.10.4239;
RA Matsui M., Stoop C.D., von Arnim A.G., Wei N., Deng X.-W.;
RT "Arabidopsis COP1 protein specifically interacts in vitro with a
RT cytoskeleton-associated protein, CIP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4239-4243(1995).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY OSMOTIC
RP STRESS AND ABSCISIC ACID, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27372427; DOI=10.1016/j.bbrc.2016.06.147;
RA Ren C., Zhu X., Zhang P., Gong Q.;
RT "Arabidopsis COP1-interacting protein 1 is a positive regulator of ABA
RT response.";
RL Biochem. Biophys. Res. Commun. 477:847-853(2016).
CC -!- FUNCTION: Positive regulator of abscisic acid (ABA)-mediated signaling
CC pathways involved in abiotic stress responses (e.g. osmotic stress) and
CC leading to various plant adaptation (e.g. stomata closure).
CC {ECO:0000269|PubMed:27372427}.
CC -!- SUBUNIT: Interacts with COP1 coiled-coil region.
CC {ECO:0000269|PubMed:7753789}.
CC -!- INTERACTION:
CC F4JZY1; P43254: COP1; NbExp=3; IntAct=EBI-2119970, EBI-301649;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27372427}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7753789}. Note=Associated
CC to the cytoskeleton in hypocotyl and cotyledon cells, but not in root
CC cells, where observed as disconnected cytoplasmic speckles
CC (PubMed:7753789). Localized to the plasma membrane in the epidermal
CC cells of cotyledons and roots, including root hairs (PubMed:27372427).
CC {ECO:0000269|PubMed:27372427, ECO:0000269|PubMed:7753789}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in photosynthetic and vascular
CC tissues. Accumulates in both dark-grown and light-grown seedlings roots
CC and shoots, leaves and flowers (at protein level).
CC {ECO:0000269|PubMed:27372427}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, accumulates in cotyledons and the
CC hypocotyl, especially in the vein. In adult plants, mainly detected in
CC mature leaves, particularly in vascular tissues. Also present in the
CC vein of sepals and petals of flowers. {ECO:0000269|PubMed:27372427}.
CC -!- INDUCTION: Induced by osmotic stress (e.g. mannitol) and abscisic acid
CC (ABA). {ECO:0000269|PubMed:27372427}.
CC -!- DISRUPTION PHENOTYPE: Short hypocotyls. Increased sensitivity to
CC osmotic stress (e.g. mannitol), but reduced sensitivity to abscisic
CC acid (ABA) associated with lower levels of abiotic stress-related gene
CC expression but higher ABA biosynthesis genes levels.
CC {ECO:0000269|PubMed:27372427}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49006.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB10654.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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 EMBL; AB016871; BAB10654.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94729.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68798.1; -; Genomic_DNA.
DR EMBL; U20810; AAC49006.1; ALT_INIT; mRNA.
DR RefSeq; NP_001330520.1; NM_001344421.1.
DR RefSeq; NP_198994.2; NM_123544.3.
DR AlphaFoldDB; F4JZY1; -.
DR SMR; F4JZY1; -.
DR IntAct; F4JZY1; 1.
DR STRING; 3702.AT5G41790.1; -.
DR iPTMnet; F4JZY1; -.
DR PaxDb; F4JZY1; -.
DR PRIDE; F4JZY1; -.
DR ProteomicsDB; 246946; -.
DR EnsemblPlants; AT5G41790.1; AT5G41790.1; AT5G41790.
DR EnsemblPlants; AT5G41790.2; AT5G41790.2; AT5G41790.
DR GeneID; 834184; -.
DR Gramene; AT5G41790.1; AT5G41790.1; AT5G41790.
DR Gramene; AT5G41790.2; AT5G41790.2; AT5G41790.
DR KEGG; ath:AT5G41790; -.
DR Araport; AT5G41790; -.
DR TAIR; locus:2152985; AT5G41790.
DR eggNOG; ENOG502QWGN; Eukaryota.
DR HOGENOM; CLU_250597_0_0_1; -.
DR InParanoid; F4JZY1; -.
DR OMA; SETHETH; -.
DR OrthoDB; 893811at2759; -.
DR PRO; PR:F4JZY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JZY1; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042306; P:regulation of protein import into nucleus; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR InterPro; IPR011684; NAB.
DR PROSITE; PS51774; NAB; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Leucine-rich repeat; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1586
FT /note="COP1-interactive protein 1"
FT /id="PRO_0000441893"
FT DOMAIN 10..84
FT /note="NAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01110"
FT REPEAT 173..187
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 188..210
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 216..239
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 261..285
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 287..309
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 384..410
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 437..461
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 473..498
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 560..586
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 613..637
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 649..674
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 768..792
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 824..850
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 856..880
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 902..929
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 944..968
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 990..1014
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 1077..1101
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 1120..1144
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 1195..1220
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 1247..1272
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 1372..1396
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 1398..1417
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 1426..1448
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 1450..1474
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 128..411
FT /evidence="ECO:0000255"
FT COILED 437..1196
FT /evidence="ECO:0000255"
FT COILED 1225..1336
FT /evidence="ECO:0000255"
FT COILED 1372..1406
FT /evidence="ECO:0000255"
FT COILED 1496..1530
FT /evidence="ECO:0000255"
FT COMPBIAS 103..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 496
FT /note="L -> K (in Ref. 3; AAC49006)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="E -> Q (in Ref. 3; AAC49006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1586 AA; 181978 MW; FD6D862810164550 CRC64;
MKKHKFRETL KSFFEPHFDH EKGEMLKGTK TEIDEKVNKI LGMVESGDVN EDESNRQVVA
DLVKEFYSEY QSLYRQYDDL TGEIRKKVNG KGESSSSSSS DSDSDHSSKR KVKRNGNGKV
EKDVELVTGA LKQQIEAANL EIADLKGKLT TTVEEKEAVD SELELALMKL KESEEISSKL
KLETEKLEDE KSIALSDNRE LHQKLEVAGK TETDLNQKLE DIKKERDELQ TERDNGIKRF
QEAEKVAEDW KTTSDQLKDE TSNLKQQLEA SEQRVSELTS GMNSAEEENK SLSLKVSEIS
DVIQQGQTTI QELISELGEM KEKYKEKESE HSSLVELHKT HERESSSQVK ELEAHIESSE
KLVADFTQSL NNAEEEKKLL SQKIAELSNE IQEAQNTMQE LMSESGQLKE SHSVKERELF
SLRDIHEIHQ RDSSTRASEL EAQLESSKQQ VSDLSASLKA AEEENKAISS KNVETMNKLE
QTQNTIQELM AELGKLKDSH REKESELSSL VEVHETHQRD SSIHVKELEE QVESSKKLVA
ELNQTLNNAE EEKKVLSQKI AELSNEIKEA QNTIQELVSE SGQLKESHSV KDRDLFSLRD
IHETHQRESS TRVSELEAQL ESSEQRISDL TVDLKDAEEE NKAISSKNLE IMDKLEQAQN
TIKELMDELG ELKDRHKEKE SELSSLVKSA DQQVADMKQS LDNAEEEKKM LSQRILDISN
EIQEAQKTIQ EHMSESEQLK ESHGVKEREL TGLRDIHETH QRESSTRLSE LETQLKLLEQ
RVVDLSASLN AAEEEKKSLS SMILEITDEL KQAQSKVQEL VTELAESKDT LTQKENELSS
FVEVHEAHKR DSSSQVKELE ARVESAEEQV KELNQNLNSS EEEKKILSQQ ISEMSIKIKR
AESTIQELSS ESERLKGSHA EKDNELFSLR DIHETHQREL STQLRGLEAQ LESSEHRVLE
LSESLKAAEE ESRTMSTKIS ETSDELERTQ IMVQELTADS SKLKEQLAEK ESKLFLLTEK
DSKSQVQIKE LEATVATLEL ELESVRARII DLETEIASKT TVVEQLEAQN REMVARISEL
EKTMEERGTE LSALTQKLED NDKQSSSSIE TLTAEIDGLR AELDSMSVQK EEVEKQMVCK
SEEASVKIKR LDDEVNGLRQ QVASLDSQRA ELEIQLEKKS EEISEYLSQI TNLKEEIINK
VKVHESILEE INGLSEKIKG RELELETLGK QRSELDEELR TKKEENVQMH DKINVASSEI
MALTELINNL KNELDSLQVQ KSETEAELER EKQEKSELSN QITDVQKALV EQEAAYNTLE
EEHKQINELF KETEATLNKV TVDYKEAQRL LEERGKEVTS RDSTIGVHEE TMESLRNELE
MKGDEIETLM EKISNIEVKL RLSNQKLRVT EQVLTEKEEA FRKEEAKHLE EQALLEKNLT
MTHETYRGMI KEIADKVNIT VDGFQSMSEK LTEKQGRYEK TVMEASKILW TATNWVIERN
HEKEKMNKEI EKKDEEIKKL GGKVREDEKE KEMMKETLMG LGEEKREAIR QLCVWIDHHR
SRCEYLEEVL SKTVVARGQR RVSQRT
