ID D7FQ17_ECTSI Unreviewed; 3821 AA.
AC D7FQ17;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=C2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Esi_0002_0104 {ECO:0000313|EMBL:CBJ48349.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ48349.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ48349.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; FN648375; CBJ48349.1; -; Genomic_DNA.
DR STRING; 2880.D7FQ17; -.
DR EnsemblProtists; CBJ48349; CBJ48349; Esi_0002_0104.
DR eggNOG; KOG0045; Eukaryota.
DR eggNOG; KOG4626; Eukaryota.
DR InParanoid; D7FQ17; -.
DR OMA; NRFKLMS; -.
DR OrthoDB; 51463at2759; -.
DR Proteomes; UP000002630; Chromosome LG02.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00030; C2; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 2.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..3821
FT /note="C2 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003095798"
FT TRANSMEM 1652..1671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1718..1745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1751..1770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1782..1801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1821..1838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1953..1970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2027..2046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2082..2101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2121..2144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2165..2189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2195..2214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2498..2516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2528..2547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2559..2578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2590..2608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2645..2664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2670..2692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2713..2746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2794..2812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2819..2840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 224..257
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 296..329
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1036..1069
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1334..1457
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 3255..3570
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 671..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2315..2344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3787..3821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3787..3810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3512
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 3821 AA; 409392 MW; B2F36020659E83E2 CRC64;
MLKSALTSAL SACLAVFTTL LYQQWASPSP QLQQQHVPVA TKIDREQELA GSPSTAPPWP
TTVDLAQALG LGRVLLSRGE HEEAALVYRV AASAAAAVDS NREHGEAQHG LGLALLATGR
PEEALVACRE AERLDPDLPT ATSCIGAILT DAGDIAGALT ALRHAADKTE RGEVTAGLWR
DAEGTADTIH GRLGAALLAA GEVDEAIEVL TRVELEARRA GGDPHAAYNL GVAWQTKGET
EKAIVAYSRA TDLAPTLAAP RVNLGAQLLQ SGRLAEAEAV LLSAAERARD DPISLAATYS
NLGAVFQRSG KPEEALESYS RAVQSGAGRP SLVHIAKLHH ELGQLEQARE ACRRAMLEEG
DSLDASPLLV TGVILESLGN VGEAADHFSK VVHQDAENVE ATMHLGACQQ RLGQHHEGPS
GKPGRCFCLR NRKKPLPVNG FKTTYVYPAF ESYTAPVIVK GGLRDVQPFE RAICTGHWLV
YRTPPAETGA AEMSQVSTAL ACFGGGEGDA EAKDAAVANP ADETLVSHDP STDGIIGAQP
SEGIGGGEDE GIAMVVDGNG LATGTLETHA EGTPARSSGT ESSAPAKAAY LDSDIVEEEL
AARDDDNIGS TVAGSIGNQG TADDIEQGEK HVLPSGTELP LPNGNGNVES TAVVDLDQAE
AEADALATLK NKLGSSSKEG EGGERGPAVP GLEVPVVEEE EEEKERQANG RTVPATAAER
EFASPPLNDA NGEQTPDGAA DADNEEDDGL TGLVEENGSV DGGSDSFEEG DIATRDPVAD
VIHPAEPSLA SAKSDTVSGD GHDIATRLGN DNPVGTEDDV TAPAGGSVDA VSEKSVDEEA
VHTLGEKAVV QGETEGAEAR RDSHEQEVVD GVGAADVTVD TQSEELDLPP TAVDTPGTSG
GFLSEQITNS LGEQAKEGIS EESIDGDNIE QVSSSPGEHA KGSITKDSMD GDDIVEARAP
ATIEVGAADD ETDEAMGGNS RSSGDASGGS GDTPATEVPK GPESDETEAG TADSADAVAE
VPVSPIVVSE DDVKRARAKA KLGMAKLQQG QAKKAVSLFE KAASIDPGWW GGFYYAALAH
DALGNAEAAA GALVSALSVP APTEENEVAG LSALSSKVLA ALDRGKQVPV AAVLKTAMDT
SGLTFAVAPP THDPPSQRDL GNSGNTNSVS PQGTGVGERT ANMGGSAGVE RAKSRDTASR
PGRDADLASQ FGRADGAAGA IPSREGRARE SLENIGRELP SSGQRGPAGG DDGARRAAGE
DRTYPGTGRG TGSGRPQRGL LVMTSSAGVN SFTGRRWILH RSRMAAHVRV GFFSVLLVAA
SRLQASQAAF TCSGGYTSCP DKNLQSHSSG GRVHAILHRA INLPDADIHQ QSGLSDPYVK
FSVGANAAQS SVVDGNLNPQ WQEEIDLGFH NSGEVVTIEV VDSDSGLEFG DDLLYSVDVR
VPWCSAFHAN ATTADCGEEY AYNCDVQGMA WAMPTQPWCN ETSWVYLGST SDSDGGEADC
GDDQTEFSCL WLEFTIIPFQ VEVENTYEGD QFLVTVADYD GDFANDPAYD DYGVVYRNIP
QLLDVNGGLF DEIRGGIMVR PDNTVAGTSG GGKVVDFSIN ADSTVWVCKW DEDTTTYGDP
SWLTEEGWQS TSAESLTGYS HNLDSKAFWN RFLEHIFAVL FFAWLSAGFL ARKEFRVDLT
EAHLMETAVA QGKQRNVLRH LLATHGKSEK NAVFRRNLCL AAFSTRLSLL VPVVALWAWG
LAIVITVNPP AVGFLFCFIG TSLIMGWNGY NHWKSRGWMM TWPSLVCILG AVFFLMAFLA
AEVFVDPAAY FGSGDLDFCG LTGIFLTLDM FPLVFLLFSN DAKLQRSVNK LGAVVGQVTR
LEELKGTNSK FSPTLKRTLS EEMMLNMGEV ERPGPKGDDA GDAGELMAKN PFYSLLGDCY
TIVASIKTFR FSDLLSATMR TSLTKKKRRD RSLYALSVLF LLAYLTVSAA RTSHAHLSLL
NIITLVLLDS CHYSIHRGST YWSPGYGVML MAAARVSIIA FMSNLWIVGY SIAFVIYGGA
LIRAVVTHRL PRLNQEEAGA VVFLGHDPKG IKCDDIAANP ELVLGYTSLY FVLVLVVLAY
AEPSGLPTPS IRVWGQEWPA YIFTLTGVLV VMSSGLFVAC LRSLSLGKQG LLPAKLGAAY
MWHPAVRLPT ILAAATGFSV LCTGLLVWAA TGSSAAFKVS LCLPAIVLLG RSTYSRWVKN
DYELVRWPPD VEKDKAAGIH VAGEEQEDHT PDAAQLAAGM LGDLFSPGDF GASDGGGFKD
EGGGKQGIIL PEFRPTGDAF TGDIQMPVLP LKSALQRTRA AQQRGAGPGG GGNEGAGLLN
NEAYDGDGDE GVGAAFAQSE EKALVRPKYV RKQQGDYAAA GAAGDVGREG GAGGEEVGVW
IRAGVALSRF LDGKGSLGVL CRKCRRRKKI GAFEGGVDGE GEIGEGDVGY GTLPGSDGNG
GGNHGDNADE ELGEVRVDSL SFRRAFLEGY LLPHEYRACY GFAACVALTV VMGLLLSREH
QGWMGHLLWT GMLVVAFTFI PAAKWFGTYE VDTTMKLSLW LAGIILTTTC ALTFVLLLDA
EAFRDQSLAV LNALLAYPIV VYSAFSCYQA MDGPTPERVS SNFDDNGEEM EEPPSKCATL
YHKTVGRFVS FKALLAVVTA LWLWQSFLWG GMYTGCGLTV AVALAGMVGL IIRDYLSQGS
MVSRSNIRGT VRLFADTVMI ACLAAALWGV GAEAFCLTVF FVVWILRIAL PVATRWLEAE
PDTVIYFAPW VFPAYTYDPR TGNLVDETHV TRQAFSGLLV GVAWGIAVAI FVEPLGIGVA
IACVFMMALA SAVAWCVSFS PNRLGVAAQF LDSSLVFEAG DVARSCFVSR HAVFEVECEE
FADQTNKGYR GADGRINPAS NAARMFEARE SAVDLAVGLE EKNKALRVVL DEETGIYETR
SDSLYSFGEA VMEAWVSGKG PLGPIGCFGL WFGILRLFAL VGHVCCRKLG AAHNPILARY
LPDGQRRDAN TLSPPIDHPD ILLEILDNES VFRGAFREEL MCMMHFQILV LLSAEARLQR
EGILFRKFLK ENHFKLLSNG IVPPNAVFSS ASFASVNIPM MAVWLTGLTG EERERFQALR
RKFSEIQSDR DRAVIEADEA CDKAAAELEK GREARSNKMA AKQRETFARR RAERADAWTE
QLAIQDQQMF ASLRAQWLKH DNVTVHPTHK LLREGFEREV LLHGEEVETN ARESLEDIES
QGRGCRPGAY GRKLQYADPD FPPDNSSVGN AQCRQQLASQ WKVSLAVNPD IRLFDDGTDP
DDVRRGAFAD SWLLSALSII SAASVGDGGV DEQIAQLFVS PIGGDGRPVL ESYTGAYAVK
ITVGGKWQVV IVDDYFPALE TSQADDDNKG LAVGHSYGAR ELWVSLLEKA YAKFFGSYAA
LETGHVHHAL SAFTGAQSEE IFLAGAGRGV GKKSLWKKMT KYKRNGYLLG AGTITGNLVE
KQVQDIGLVF GAAYTILDVR DSDGEQLIKL RNPPGDHEEW RGDWGDNSML WTRRRRARLG
LVKNDKDNAF WMSFNDFCVV FRSLYVCRWY DPRRWTRLEQ SGSWEMREDL DTAAGLPSAQ
QKVCELENNP QFVLEVNRIT DLKISLIQTD DEVQPAACFV LREDEATSST QPERFPARVS
RLSREVVVAS TGPPARQRER NIYVTLASGT YVVMCAAFLA GMEGSFKVEI TTNSPQLKFR
KLWPPADPSE LEKAFDDSKA AGRIANMGLE KLGAMSAGLG DKLNDNADKA LNKARALEMG
LKVAAAREKE ERVKEDAELD AEDGRGRQQE QQQRVVENPY P
//
