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Protein

Protein piccolo

Gene

Pclo

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri523 – 54725C4-type1 PublicationSequence analysisAdd
BLAST
Zinc fingeri1010 – 103324C4-type1 PublicationSequence analysisAdd
BLAST

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • profilin binding Source: UniProtKB
  • transcription corepressor binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • synapse assembly Source: InterPro
  • synaptic vesicle targeting Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein piccolo
Alternative name(s):
Aczonin
Multidomain presynaptic cytomatrix protein
Gene namesi
Name:Pclo
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69406. Pclo.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • cone cell pedicle Source: RGD
  • cytoskeleton of presynaptic active zone Source: RGD
  • dendrite Source: RGD
  • growth cone Source: RGD
  • inhibitory synapse Source: RGD
  • neuromuscular junction Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • presynaptic active zone Source: RGD
  • ribbon synapse Source: RGD
  • rod spherule Source: RGD
  • synapse Source: UniProtKB
  • terminal bouton Source: RGD
  • trans-Golgi network Source: RGD
  • transport vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4668 – 46681D → A: Complete loss of calcium-binding and calcium-dependent phospholipid binding activity. 1 Publication
Mutagenesisi4674 – 46741D → A: Complete loss of calcium-binding and calcium-dependent phospholipid binding activity. 1 Publication
Mutagenesisi4688 – 46892VM → SS: 10-fold increase in affinity for calcium. 1 Publication
Mutagenesisi4688 – 46881V → S: Small increase in affinity for calcium. 1 Publication
Mutagenesisi4689 – 46891M → S: Increased affinity for calcium. 1 Publication
Mutagenesisi4690 – 46912VV → SS: 10-fold increase in affinity for calcium. 1 Publication
Mutagenesisi4692 – 46932QN → AA: Moderate increase in affinity for calcium. 1 Publication
Mutagenesisi4694 – 46941A → S: No effect on calcium-binding activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 50855085Protein piccoloPRO_0000058252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei857 – 8571PhosphoserineBy similarity
Modified residuei869 – 8691PhosphoserineBy similarity
Modified residuei873 – 8731PhosphothreonineBy similarity
Modified residuei1133 – 11331PhosphothreonineBy similarity
Modified residuei1304 – 13041PhosphoserineCombined sources
Modified residuei1314 – 13141PhosphoserineBy similarity
Modified residuei1315 – 13151PhosphoserineBy similarity
Modified residuei1344 – 13441PhosphoserineBy similarity
Modified residuei1346 – 13461PhosphoserineCombined sources
Modified residuei1349 – 13491PhosphoserineBy similarity
Modified residuei1350 – 13501PhosphoserineBy similarity
Modified residuei1353 – 13531PhosphoserineCombined sources
Modified residuei1451 – 14511PhosphoserineCombined sources
Modified residuei1463 – 14631PhosphoserineCombined sources
Modified residuei1464 – 14641PhosphoserineCombined sources
Modified residuei1466 – 14661PhosphoserineBy similarity
Modified residuei1469 – 14691PhosphoserineCombined sources
Modified residuei1493 – 14931PhosphoserineCombined sources
Modified residuei1496 – 14961PhosphoserineCombined sources
Modified residuei1517 – 15171PhosphoserineCombined sources
Modified residuei1519 – 15191PhosphoserineCombined sources
Modified residuei1564 – 15641PhosphothreonineBy similarity
Modified residuei1565 – 15651PhosphoserineBy similarity
Modified residuei1575 – 15751PhosphoserineBy similarity
Modified residuei1587 – 15871PhosphoserineBy similarity
Modified residuei1650 – 16501PhosphoserineCombined sources
Modified residuei1652 – 16521PhosphothreonineCombined sources
Modified residuei1654 – 16541PhosphoserineCombined sources
Modified residuei1659 – 16591PhosphoserineBy similarity
Modified residuei1720 – 17201PhosphoserineBy similarity
Modified residuei1721 – 17211PhosphoserineCombined sources
Modified residuei1772 – 17721PhosphothreonineBy similarity
Modified residuei1778 – 17781PhosphoserineBy similarity
Modified residuei1807 – 18071PhosphoserineBy similarity
Modified residuei1812 – 18121PhosphoserineCombined sources
Modified residuei1820 – 18201PhosphoserineCombined sources
Modified residuei1841 – 18411PhosphoserineCombined sources
Modified residuei2511 – 25111PhosphoserineBy similarity
Glycosylationi2702 – 27021O-linked (GlcNAc)By similarity
Glycosylationi2976 – 29761O-linked (GlcNAc)By similarity
Modified residuei3014 – 30141PhosphothreonineBy similarity
Modified residuei3374 – 33741PhosphoserineBy similarity
Modified residuei3388 – 33881PhosphoserineBy similarity
Modified residuei3392 – 33921PhosphothreonineCombined sources
Modified residuei3419 – 34191PhosphothreonineCombined sources
Modified residuei3522 – 35221PhosphoserineBy similarity
Modified residuei3530 – 35301PhosphoserineBy similarity
Modified residuei3561 – 35611PhosphoserineBy similarity
Modified residuei3565 – 35651PhosphoserineBy similarity
Modified residuei3571 – 35711PhosphoserineCombined sources
Modified residuei3574 – 35741PhosphoserineCombined sources
Modified residuei3577 – 35771PhosphoserineCombined sources
Modified residuei3598 – 35981PhosphoserineCombined sources
Modified residuei3624 – 36241PhosphoserineCombined sources
Modified residuei3626 – 36261PhosphoserineCombined sources
Modified residuei3632 – 36321PhosphoserineCombined sources
Modified residuei3781 – 37811PhosphoserineCombined sources
Modified residuei4034 – 40341PhosphoserineCombined sources
Modified residuei4150 – 41501PhosphoserineCombined sources
Modified residuei4304 – 43041PhosphoserineBy similarity
Modified residuei4308 – 43081PhosphoserineBy similarity
Modified residuei4311 – 43111PhosphoserineBy similarity
Modified residuei4340 – 43401PhosphoserineCombined sources
Modified residuei4376 – 43761PhosphoserineBy similarity
Modified residuei4609 – 46091PhosphoserineBy similarity
Modified residuei4723 – 47231PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9JKS6.
PRIDEiQ9JKS6.

PTM databases

iPTMnetiQ9JKS6.
PhosphoSiteiQ9JKS6.

Interactioni

Subunit structurei

Interacts with RABAC1/PRA1, RIMS2 and profilin.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Siah1Q920M92EBI-2271602,EBI-957514

GO - Molecular functioni

  • profilin binding Source: UniProtKB
  • transcription corepressor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

IntActiQ9JKS6. 1 interaction.
STRINGi10116.ENSRNOP00000008637.

Structurei

Secondary structure

1
5085
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4642 – 46509Combined sources
Beta strandi4653 – 466311Combined sources
Beta strandi4668 – 46714Combined sources
Beta strandi4676 – 46816Combined sources
Helixi4696 – 46994Combined sources
Turni4700 – 47056Combined sources
Helixi4706 – 47094Combined sources
Beta strandi4712 – 47198Combined sources
Helixi4724 – 47274Combined sources
Beta strandi4731 – 47399Combined sources
Beta strandi4741 – 47433Combined sources
Beta strandi4745 – 475410Combined sources
Helixi4759 – 47613Combined sources
Beta strandi4766 – 47694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH8NMR-A4635-4776[»]
ProteinModelPortaliQ9JKS6.
SMRiQ9JKS6. Positions 4430-4538, 4635-4776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JKS6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4442 – 453695PDZPROSITE-ProRule annotationCuratedAdd
BLAST
Domaini4653 – 4752100C2 1PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini4968 – 505992C2 2PROSITE-ProRule annotationCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni372 – 49112012 X 10 AA tandem approximate repeats of P-A-K-P-Q-P-Q-Q-P-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2351 – 236212Poly-ProCuratedAdd
BLAST

Domaini

C2 domain 1 is involved in binding calcium and phospholipids. Calcium binds with low affinity but with high specificity and induces a large conformational change.1 Publication

Sequence similaritiesi

Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri523 – 54725C4-type1 PublicationSequence analysisAdd
BLAST
Zinc fingeri1010 – 103324C4-type1 PublicationSequence analysisAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2060. Eukaryota.
ENOG410ZNB1. LUCA.
HOGENOMiHOG000168263.
HOVERGENiHBG031058.
InParanoidiQ9JKS6.
KOiK16882.
PhylomeDBiQ9JKS6.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.40.150. 2 hits.
3.30.40.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR001478. PDZ.
IPR030629. Piccolo.
IPR011011. Znf_FYVE_PHD.
IPR008899. Znf_piccolo.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR14113:SF6. PTHR14113:SF6. 2 hits.
PfamiPF00168. C2. 2 hits.
PF00595. PDZ. 1 hit.
PF05715. zf-piccolo. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF50156. SSF50156. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50004. C2. 2 hits.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JKS6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGNEASLEGE GLPEGLAAAA GAGGSGSALH PGIPAGMEAD LSQLSEEERR
60 70 80 90 100
QIAAVMSRAQ GLPKGSVPPA AAESPSMHRK QELDSSQAPQ QPGKPPDPGR
110 120 130 140 150
PTQPGLSKSR TTDTFRSEQK LPGRSPSTIS LKESKSRTDF KEEYKSSMMP
160 170 180 190 200
GFFSDVNPLS AVSSVVNKFN PFDLISDSEA SQEETTKKQK VVQKEQGKSE
210 220 230 240 250
GMAKPPLQQP SPKPIPKQQG QVKEVIQQDS SPKSVSSQQA EKVKPQAPGT
260 270 280 290 300
GKPSQQSPAQ TPAQQASPGK PVAQQPGSAK ATVQQPGPAK SPAQPAGTGK
310 320 330 340 350
SPAQPPAKTP GQQAGLEKTS SSQQPGPKSL AQTPGHGKFP LGPVKSPAQQ
360 370 380 390 400
PGTAKHPAQQ PGPQTAAKVP GPTKTPAQQS GPGKTPAQQP GPTKPSPQQP
410 420 430 440 450
IPAKPQPQQP VATKTQPQQS APAKPQPQQP APAKPQPQQP TPAKPQPQPP
460 470 480 490 500
TPAKPQPQPP TATKPQPQPP TATKPHHQQP GLAKPSAQQP TKSISQTVTG
510 520 530 540 550
RPLQPPPTSA AQTPAQGLSK TICPLCNTTE LLLHIPEKAN FNTCTECQST
560 570 580 590 600
VCSLCGFNPN PHLTEIKEWL CLNCQMQRAL GGDLAAAIPS SPQPTPKAAT
610 620 630 640 650
APTATASKSP VPSQQASPKK EPPSKQDSPK ALESKKPPEP KKPPEPKKPP
660 670 680 690 700
EPKKPPPLVK QPTLHGPTPA TAPQLPVAEA LPEPAPPKEP SGPLPEQAKA
710 720 730 740 750
PVGDVEPKQP KMTETRADIQ SSSTTKPDIL SSQVQSQAQV KTASPLKTDS
760 770 780 790 800
AKPSQSFPPT GEKTTPLDSK AMPRPASDSK IISQPGPGSE SKDPKHIDPI
810 820 830 840 850
QKKDEPKKAQ PKGSPKPETK PVPKGSPTPS GTRPTAGQAA PPSQQPPKPQ
860 870 880 890 900
EQSRRFSLNL GGITDAPKSQ PTTPQETVTG KLFGFGASIF SQASNLISTA
910 920 930 940 950
GQQGPHPQTG PAAPSKQAPT PSQSPAAQGP AKSTGQLPPA PAKATAVKKE
960 970 980 990 1000
AKAAAAENLE SKPEQAPTAK KTEKDKKPPP AKVGKPPPSE PEKAVPAHKP
1010 1020 1030 1040 1050
DKTTKPKPAC PLCRTELNLG SQEPPNFNTC TECKNQVCNL CGFNPTPHLT
1060 1070 1080 1090 1100
EIQEWLCLNC QTQRAISGQL GDMGKMPPAP SGPKASPMPA PAEPSSQKTP
1110 1120 1130 1140 1150
TGTQVKGKKK EAEGKTEAEK PVPEKETASI EKTPPMVTTD QKLEESEGKK
1160 1170 1180 1190 1200
SKVSALPEKK PSEEEKAISA DKKERKPPAE EKPPLEEKKP IPVDKKLPPE
1210 1220 1230 1240 1250
AKPLSSEGEE KHEILKAHVQ IPEEEPTGKV AAKAGEEEQQ PDSRPEALPG
1260 1270 1280 1290 1300
ATPLTLPKAG EKERAVAQPQ AEGSSKDGQG ERSKEKTEKE EDKSDTSSSQ
1310 1320 1330 1340 1350
QPKSPQGLSD TGYSSDGISG SLGEIPSLIP SDEKDLLKGL KKDSFSQESS
1360 1370 1380 1390 1400
PSSPSDLAKL ESTVLSILEA QASTLVGEKA EKKTQPQKIS PEKPQDQQKT
1410 1420 1430 1440 1450
QTASETLDIT ISEEEIKESQ EKKVSPKKDS EQGFPSRKEH KEKPELVDDL
1460 1470 1480 1490 1500
SPRRASYDSV EDSSESENSP VVRRKRRTSI GSSSSDEYKQ EDSQGSGEEE
1510 1520 1530 1540 1550
DFIRKQIIEM SADEDASGSE DEEFIRSQLK EISGVGESQK REEAKGKGKG
1560 1570 1580 1590 1600
VAGKHRRLTR KSSTSFDDDA GRRHSWHDED DETFDESPEL KFRETKSQES
1610 1620 1630 1640 1650
EELVVAGGGG LRRFKTIELN STIADKYSSE SSQKKTILYF DEEPELEMES
1660 1670 1680 1690 1700
LTDSPEDRSR GEGSSSLHAS SFTPGTSPTS VSSLDEDSDS SPSHKKGESK
1710 1720 1730 1740 1750
QQRKARHRSH GPLLPTIEDS SEEEELREEE ELLKEQEKQR ELEQQQRKSS
1760 1770 1780 1790 1800
SKKSKKDKDE LRAQRRRERP KTPPSNLSPI EDASPTEELR QAAEMEELHR
1810 1820 1830 1840 1850
SSCSEYSPSI ESDPEGFEIS PEKIIEVQKV YKLPAAVSLY SPTDEQSVMQ
1860 1870 1880 1890 1900
KEGVQKALKS AEEMYEEMMQ KPHKYKAFPA ANERDEVFEK EPLYGGMLIE
1910 1920 1930 1940 1950
DYIYESLVED TYNGSVDGSL LTRQEEQNGF MQQRGREQKV RLQEQIYDDP
1960 1970 1980 1990 2000
MQKISDLQKE FYELESLHSV VPQEDIVSSS YIIPESHEIV DLGSMVMSTS
2010 2020 2030 2040 2050
EEKKLLDADS AYEELMRRQQ VQVTDGSSPV QTTIGDDMAE STLDFDRVQD
2060 2070 2080 2090 2100
ASLTSSILSG ASLTDSTSSA TLSIPDVKIT QQFSAEELED EYVTDYTREI
2110 2120 2130 2140 2150
QDIIAHESLI LTYSEPSESA TSVPPSDTPS LTSSISSVCT TDSSSPVTTL
2160 2170 2180 2190 2200
DSLTTVYTEP ADVMTKFKDS EEISSTYFPG SIIDYPEDIS VSLDRTIMPE
2210 2220 2230 2240 2250
SRTNEDRIVL SFSGMAPSVV ESVGTKPERP QADTISTDLP ISEKDLIKGK
2260 2270 2280 2290 2300
KETGDGIILE VLDAYKDKRE ESEAELTKIS LPEPGLAQAP SSVTAPQIKE
2310 2320 2330 2340 2350
QHVSPHSVSG KISGQEKPTY RLPSGSLPVS THPSKSRPFF RSSSLDISAQ
2360 2370 2380 2390 2400
PPPPPPPPPP SPSTSSPPPT PPLPPATSPK PPTYPKKKLA VAATVTSTTI
2410 2420 2430 2440 2450
VTTHVDALTM VEAAAARRSN GLPATKMCAI APPPVPPKPS QIPTGLVFTH
2460 2470 2480 2490 2500
RPEAIKPPIA PKPAVPQIPV TTQKPTDTCP KPTGLSLTST MSLNLVTSAD
2510 2520 2530 2540 2550
YNVPSPTSPL SPHSNKSSPR YSKSLMDTYV VITLPSEPGT PTDSSAAQAI
2560 2570 2580 2590 2600
TSWPLGSPPK DLVSLETVFS VVPPMTSTEI PSASQPTLYT SGALGTFSVT
2610 2620 2630 2640 2650
PAVTASLFQT VPTSLTQFLP AEASKPEVSA VSSAVPSVAP RSVSIPIPPE
2660 2670 2680 2690 2700
PLALDRHQYK ENGKLPLIGD AIDLRTIPKS EVKVTEKCMD LSASAMDVKR
2710 2720 2730 2740 2750
QTTANEVYRR QISAVQPSII NLSAASSLGT PVTMDSKTVA VVTCTDTTIY
2760 2770 2780 2790 2800
TTGTESQVGI EHAVTSPLQL TTSKHTELPY RKPSSQAFPT IRDEAPINLS
2810 2820 2830 2840 2850
LGPSAQAVTL AVTKPVTVPP VGVTNGWTDS TLSQGVADGE VVDLSTSKSH
2860 2870 2880 2890 2900
RTVVTMDEST SNVVTKIIED DEKPVDLTAG RRAVCCDMVY TLPFGRSCTA
2910 2920 2930 2940 2950
QQPATTLPED RFGYRDDHYQ YDRSGPYGYR GIGGMKPSMS DTNLPEAGHF
2960 2970 2980 2990 3000
FYKSKNAFDY SGGTGAAVDL TSGRVSTGEV MDYSSKTTGP YPETRQVISG
3010 3020 3030 3040 3050
VGISTPQYST ARLTPPPGPQ YGVGSVLRSS NGVVYSSVAT PIPSTFAITT
3060 3070 3080 3090 3100
QPGSIFSTTV RDLSGIPTTD AMTSLSALHQ SQPMPRSYFI TTGASETDIA
3110 3120 3130 3140 3150
VTGIDINASL QTITMETLPA ETMDSVPTLT TASEVFSEVV GEESTLLIVP
3160 3170 3180 3190 3200
DEDKQQQQLD LERELLELEK IKQQRFAEEL EWERQEIQRF REQEKIMVQK
3210 3220 3230 3240 3250
KLEELQSMKQ HLLYQQEEER QAQFMMRQET LAQQQLQLEQ IQQLQQQLHQ
3260 3270 3280 3290 3300
QLEEQKLRQI YQYNYDPSGT SSPQTTTEQA ILEGQYAATE GSQFWATEDA
3310 3320 3330 3340 3350
TTTASTVVAI EIPQSQGWYT VQSDGVTQYI APPGILSTVS EIPLTDVVVK
3360 3370 3380 3390 3400
EEKQPKKRSS GAKVRGQYDE MGESVADDPR NLKKIVDSGV QTDDEETADR
3410 3420 3430 3440 3450
SYASRRRRTK KSVDTSVQTD DEDQDEWDMP SRSRRKARTG KYGDSTAEGD
3460 3470 3480 3490 3500
KTKPLSKVSS VAVQTVAEIS VQTEPVGTIR TPSIRARVDA KVEIIKHISA
3510 3520 3530 3540 3550
PEKTYKGGSL GCQTETDSDT QSPPYLGATS PPKDKKRPTP LEIGYSSSHL
3560 3570 3580 3590 3600
RADPTVQLAP SPPKSPKVLY SPISPLSPGN ALEPAFVPYE KPLPDDISPQ
3610 3620 3630 3640 3650
KVLHPDMAKV PPASPKTAKM MQRSMSDPKP LSPTADESSR APFQYSEGFT
3660 3670 3680 3690 3700
TKGSQTMTAS GTQKKVKRTL PNPPPEEVST GTQSTYSTMG TASRRRMCRT
3710 3720 3730 3740 3750
NTMARAKILQ DIDRELDLVE RESAKLRKKQ AELDEEEKEI DAKLRYLEMG
3760 3770 3780 3790 3800
INRRKEALLK EREKRERAYL QGVAEDRDYM SDSEVSSTRP SRVESQHGVE
3810 3820 3830 3840 3850
RPRTAPQTEF SQFIPPQTQT EAQLVPPTSP YTQYQYSSPA LPTQAPTPYT
3860 3870 3880 3890 3900
QQSHFQQQTL YHQQVSPYQT QPTFQAVATM SFTPQAQPTP TPQPSYQLPS
3910 3920 3930 3940 3950
QMMVIQQKPR QTTLYLEPKI TSNYEVIRNQ PLMIAPVSTD NTYAVSHLGS
3960 3970 3980 3990 4000
KYNSLDLRIG LEERSSMAGS PISSISADSF YADIDHHTSR NYVLIDDIGD
4010 4020 4030 4040 4050
ITKGTAALST VFSLHEKDLS KTDRLLRTTE TRRSQEVTDF LAPLQTSSRL
4060 4070 4080 4090 4100
HSYVKADEDP MEDPYELKLL KHQIKQEFRR GTESLDHLAG LSHYYHADTS
4110 4120 4130 4140 4150
YRHFPKSEKY SISRLTLEKQ AAKQLPAAIL YQKQSKHKKS LIDPKMSKFS
4160 4170 4180 4190 4200
PIQESRDLEP DYPTYMSSGT SSIGGISSRA RLLQDDITFG LRKNITDQQK
4210 4220 4230 4240 4250
FMGSSLGSGL GTLGNTIRSA LQDEADKPYS SGSRSRPSSR PSSVYGLDLS
4260 4270 4280 4290 4300
IKRDSSSSSL RLKAQEAEAL DVSFGHSSSS ARTKPTSLPI SQSRGRIPIV
4310 4320 4330 4340 4350
AQSSEEESPL SPVGQPMGMA RAAAGPLPPI SADTRDQFGS SHSLPEVQQH
4360 4370 4380 4390 4400
MREESRTRGY DRDIAFIMDD FQHAMSDSEA YHLRREETDW FDKPRESRLE
4410 4420 4430 4440 4450
NGHGLDRKLP ERLVHSRPLS QHQEQILQMN GKTIHYIFPH ARVKITRDFK
4460 4470 4480 4490 4500
DHTGSGNGLG IRIVGGKEIP GHSGEIGAYI AKILPGESAE HTGPLMEGMQ
4510 4520 4530 4540 4550
VLEWNGVPLT SKTYEEVQSI INQQSGEAEI CVRLDLNMLS DSENPQHLEL
4560 4570 4580 4590 4600
HEPPKVDKAK SPGVDPKQLA AELQKVSLQQ SPLVMSSVVE KGSHAHSGPT
4610 4620 4630 4640 4650
SAGSSSVPSP GQPGSPSVSK KKHSSTKPTD GPKAASHPIT GEIQLQINYD
4660 4670 4680 4690 4700
LGNLIIHILQ ARNLVPRDNN GYSDPFVKVY LLPGRGQVMV VQNASAEYKR
4710 4720 4730 4740 4750
RTKYVQKSLN PEWNQTVIYK SISMEQLMKK TLEVTVWDYD RFSSNDFLGE
4760 4770 4780 4790 4800
VLIDLSSTSH LDNTPRWYPL KEQTESIDHG KSHSSQNSQQ SPKPSVIKSR
4810 4820 4830 4840 4850
SHGIFPDPSK DMQVPTIEKS HSSPGSSKSS SEGHLRSHGP SRSQSKTSVA
4860 4870 4880 4890 4900
QTHLEDAGVA IAAAEAAVQQ LRIQPTKPTN HRPAESSVST GSSGSSVGSG
4910 4920 4930 4940 4950
YSVDSEGSSC VAGEPNLLPI PRIGKMGQNG QDPVKQPGMG ATDTEGKTQV
4960 4970 4980 4990 5000
MGEIKLALKK EMKTDGEQLI VEILQCRNIT YKFKSPDHLP DLYVKLYVIN
5010 5020 5030 5040 5050
ISTQKKVIKK KTRVCRHDRE PSFNETFRFS LSPAGHSLQI LLFSNGGKFM
5060 5070 5080
KKTLIGEACI WLDKVDLRKR IVNWHKLLVS PTQTH
Length:5,085
Mass (Da):552,716
Last modified:October 1, 2000 - v1
Checksum:i5A1BB543201A7450
GO
Isoform 2 (identifier: Q9JKS6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4876-4880: TKPTN → SKRRK
     4881-5085: Missing.

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Length:4,880
Mass (Da):530,153
Checksum:i73951EE4ED83EA68
GO
Isoform 3 (identifier: Q9JKS6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4687-4695: Missing.

Show »
Length:5,076
Mass (Da):551,758
Checksum:i41D97D62D0F389D9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4687 – 46959Missing in isoform 3. CuratedVSP_018194
Alternative sequencei4876 – 48805TKPTN → SKRRK in isoform 2. 1 PublicationVSP_003930
Alternative sequencei4881 – 5085205Missing in isoform 2. 1 PublicationVSP_003931Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF138789 mRNA. Translation: AAF07822.2.
AF227534 mRNA. Translation: AAF63196.1.
RefSeqiNP_001104267.1. NM_001110797.1. [Q9JKS6-2]
NP_064483.1. NM_020098.1. [Q9JKS6-1]
UniGeneiRn.53925.

Genome annotation databases

GeneIDi56768.
KEGGirno:56768.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF138789 mRNA. Translation: AAF07822.2.
AF227534 mRNA. Translation: AAF63196.1.
RefSeqiNP_001104267.1. NM_001110797.1. [Q9JKS6-2]
NP_064483.1. NM_020098.1. [Q9JKS6-1]
UniGeneiRn.53925.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH8NMR-A4635-4776[»]
ProteinModelPortaliQ9JKS6.
SMRiQ9JKS6. Positions 4430-4538, 4635-4776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JKS6. 1 interaction.
STRINGi10116.ENSRNOP00000008637.

PTM databases

iPTMnetiQ9JKS6.
PhosphoSiteiQ9JKS6.

Proteomic databases

PaxDbiQ9JKS6.
PRIDEiQ9JKS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56768.
KEGGirno:56768.

Organism-specific databases

CTDi27445.
RGDi69406. Pclo.

Phylogenomic databases

eggNOGiKOG2060. Eukaryota.
ENOG410ZNB1. LUCA.
HOGENOMiHOG000168263.
HOVERGENiHBG031058.
InParanoidiQ9JKS6.
KOiK16882.
PhylomeDBiQ9JKS6.

Miscellaneous databases

EvolutionaryTraceiQ9JKS6.
PROiQ9JKS6.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
2.60.40.150. 2 hits.
3.30.40.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR001478. PDZ.
IPR030629. Piccolo.
IPR011011. Znf_FYVE_PHD.
IPR008899. Znf_piccolo.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR14113:SF6. PTHR14113:SF6. 2 hits.
PfamiPF00168. C2. 2 hits.
PF00595. PDZ. 1 hit.
PF05715. zf-piccolo. 2 hits.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF50156. SSF50156. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEiPS50004. C2. 2 hits.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RABAC1.
  2. Fenster S.D., Cases-Langhoff C., Gundelfinger E.D., Garner C.C.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "An unusual C(2)-domain in the active-zone protein piccolo: implications for Ca(2+) regulation of neurotransmitter release."
    Gerber S.H., Garcia J., Rizo J., Suedhof T.C.
    EMBO J. 20:1605-1619(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING, MUTAGENESIS OF ASP-4668; ASP-4674; VAL-4688; 4688-VAL-MET-4689; MET-4689; 4690-VAL-VAL-4691; 4692-GLN-ASN-4693 AND ALA-4694.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-1304; SER-1346; SER-1353; SER-1451; SER-1463; SER-1464; SER-1469; SER-1493; SER-1496; SER-1517; SER-1519; SER-1650; THR-1652; SER-1654; SER-1721; SER-1812; SER-1820; SER-1841; THR-3392; THR-3419; SER-3571; SER-3574; SER-3577; SER-3598; SER-3624; SER-3626; SER-3632; SER-3781; SER-4034; SER-4150; SER-4340 AND SER-4723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "A conformational switch in the Piccolo C2A domain regulated by alternative splicing."
    Garcia J., Gerber S.H., Sugita S., Suedhof T.C., Rizo J.
    Nat. Struct. Mol. Biol. 11:45-53(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 4635-4776, ALTERNATIVE SPLICING (ISOFORM 3).

Entry informationi

Entry nameiPCLO_RAT
AccessioniPrimary (citable) accession number: Q9JKS6
Secondary accession number(s): Q9JLT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.