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Database: UniProt
Entry: R7TSZ2_CAPTE
LinkDB: R7TSZ2_CAPTE
Original site: R7TSZ2_CAPTE 
ID   R7TSZ2_CAPTE            Unreviewed;      3794 AA.
AC   R7TSZ2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CAPTEDRAFT_160045 {ECO:0000313|EMBL:ELT94606.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT94606.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT94606.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT94606.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP160045}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   EMBL; AMQN01002497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMQN01002498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB309374; ELT94606.1; -; Genomic_DNA.
DR   STRING; 283909.R7TSZ2; -.
DR   EnsemblMetazoa; CapteT160045; CapteP160045; CapteG160045.
DR   HOGENOM; CLU_000246_3_0_1; -.
DR   OMA; DWCSTLM; -.
DR   Proteomes; UP000014760; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd21187; CH_DMD-like_rpt2; 1.
DR   CDD; cd16242; EFh_DMD_like; 1.
DR   CDD; cd00176; SPEC; 9.
DR   CDD; cd00201; WW; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 1.20.58.60; -; 15.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR035436; Dystrophin/utrophin.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12268:SF14; DYSTROPHIN-1; 1.
DR   PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00435; Spectrin; 8.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF002341; Dystrophin/utrophin; 3.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 18.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          1..52
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          67..172
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          3064..3097
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          3318..3374
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          178..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1912..1939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3644..3687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3775..3794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          362..389
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          969..1003
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1170..1254
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1289..1342
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1531..1569
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2020..2084
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2619..2646
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2944..2971
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3023..3050
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3491..3525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3576..3606
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        190..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3777..3794
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3794 AA;  433023 MW;  1B1961EC87FC6A56 CRC64;
     MRVHHMNNVN RVLQILETDY NIKLVNISGN DVVEGNTKIT LGLIWSIIQH WQVKDVMKEV
     MTELRQTNLE KTLLAWCRNT TEGYPNVNIK NFTDSWRDGL AFNALMHKYH PEYFDFDSLL
     SEDINSRLQH AFRVAYDKLS IEKLLDPEDV NVDHPDKKSI VMYVTCFFQV LPHSHIVMDS
     DPDTPSEEAS LPPPSKSTSA STSSSLSQLG SPEACADLGA FNQSLEMVMT WLLQAEETLA
     QQNDVGSDVH TVKEQFHQHE EFMLQLTQHQ GSVGSVLQEG SSLLREQNIN SDDEKAIQNQ
     MSLLNNRWEG LRVTAMERQS KLQQELMEQQ QAQLNKLGSW LTEMEQKMKE CGGFVAGDVD
     VVTEQIRKQK ALQSQVEEQQ DRVNSLQNMV VVVDDTNSES ACMALEEQLE ALGQRWASVC
     KWTEEHWLLL QEMLTRWQHY NDECRLFSDW LMEKESVLAA MRLVDISELK EVVDQVRQLK
     QDMDLQVQTF DDLNDRGQEL VSFLNNDPET VQKINAQLQE FQERWDNLVQ QMEYQSKEIS
     HSGIDLQVTK GQNGSYTITV TRREGSTVIT ETITTSSSTL TSSNVGYLSA PKRPRIESKH
     RHEFESEIAS LSEWFDKTEV NIELLTMEPS DPQDQLTLEE QMVLDTERDI LSRQPHMDKF
     HSVANSFKLE LSNAGEPTEL IEEAVEQVDQ RWQGLNDLLK LTKSKVMLNH ETKQFYEELT
     SLRGILMTYE RWIGTAEGMS DEALEITKQL EQCRVKLKAM KSHEGQAEKL GKLVEDLAGR
     DVDATDTLQS IQQDLLDFTT RWQNTFTKIG ERQQQLTKAL EKAPPKSYLD AMAALLKWIE
     GVELLLQSEP FLVTESDIMQ EQLVQYRALQ GDIQDHLGNL EYINHTGKDL LTRAASGDKT
     EKLNSNLKSL NERWTEVSNS IDTRVDKLED AIAQLKQYQT QTGGLERWMA EMDVYLRTDE
     VATGDLEMVQ AQIQENEGVK EDIRTLQENL DNVNEIIADL VEIADNDFTE RLTKEVDELN
     SQWESVKVLS KEQSDRLTRG MEMTEKVHNQ IKVLEKYMDS VNREHLAHEY TVHTKEELVQ
     LNTKFKKRSQ ELEQLVKDVN SIVGDGSPGN LEPLVNSKAK VEQRWLQIRK DAEDLNMKFQ
     TCVNNLTKFK ILLSEEFRWL DTMDKRLSER PKACVDAEEI SEELDELENQ LHNHSKQQKS
     QIESTAQSLI NNHIMVAKVQ TDLEEFQTRF ESTEAKAKQR QEDLEEAIQQ AQLRESQIIE
     MTNWMDDVSG LLQSRLDADI LAGESPSEFE GLKAEFEEQE VLLKQLEQQA EEFSSEGKTE
     AAERLEQQVT ILKQHFAELE LKFCKFQRPV DFEPKLNHAK RTLSDIGERI HLIEVSSDDM
     EVLQPQMETC LKFYRTMTEL KSDVEYVIKT GRQVVEKKQV DFPDKLNAQL DALKQQYNDL
     GGQVTNGKQK LEKSVKVAKK LRRESHLLRD FLTLTDEELS NRESVRMPKD MEAEIKWIKA
     TQADLQKRQS SATNVVDLVT QLSSLAEEGT LVDAEQSMRQ LADQYQDLVD RLAARKHNLK
     EECVAQESRY IEFTTSVQEM SVWMDHVEDT LNQSEQLSHE DQVAEAEIEK FKVINSTDME
     MNFFLLGYQI RYWPIAPLRK NCHSVSPRLV HPTAASAVCP QHATAEEAAF KAIADTSWRA
     VSALHSLICR VCLRTMPPFI ERKSLSISTT PNPSYVDHNG SVMFGIYSSL FISFEIRMKL
     PLPMATNRPS HCLLSPACYG IAEFFHWSHF QTVQFEQSDF KATVDNVRDT AVDLMSRSEK
     YAKLVEPELS SLNQRWSDIS KRLQVGAQRV DYAMCYVIHV EGETEPAPRN KLRERVQGLL
     LEGEKQADDL QAKNPEEAQK IQEHAARLKT KWESVQENRE SKVVVASVTF ARSRREEDSG
     QSTEERKREE AEGDAEELKA FEDEVAEHED EMGNRMQEGD EMDGVEERCT QLTTTNSNSA
     VEASSVDEDE VVAMETSVTE MSISMTSSVC IVSTSPTEFI QGLERLLVVL EDILSELQCS
     LLHGRQYEDF SSQEDKLKSI REALDNVQSS LQTAEQRQQE ALTNANSDEN LRIAELMASV
     RQQWTVANTQ YNDRHSRWNC SVEMWGRFHC NLKDLASWLT DAEAKLQDSK NANGQLDVQV
     AKDYQKELEE AIKIHQSTVA SLNASGGEII DQSSAPDSSL LTEKLDSLNQ RWRLVCTEVS
     DRKERFEENS LSAQQLKEDL DDLTSWLRET DNIITSKLRP ADEEYLEDLL EKVKDREEEI
     SLQQNAIDTL IAAQVEDDLS VVQEQWVRVQ HGLPAKRAAA EQALSNIRMF SGDLEALSAW
     MTSSKEILEH KNSAGASSST AQGENDSIVV DPANMQEALS ARQKNMNNLT DRFEGLCKEC
     SMLGVPVPEH LQAKVDQLHA DWELVHELAS QLRPLSDTSM EESVFIEGIV LVASITRVTT
     QTVQTAVAMA TSPTTPESSS SDLESALATR HNALRAVMTS LNLRRAIVGR SEHVESRLKE
     VQEHDLGTGS SHPTLKRLVP YSSIMYTCTF PCISFSVERL REQWDEAGAK AAQRRRLLDE
     MLQDSRHLEE LRSDIERFLG QWAAECDRRP EATASVDRVE QQLQSHKKLQ EEVESFQSKV
     DDFNDHADRM AEVYSQDDLS SLKDTVSQVN AGWTSLLARL STRQKSLQNS LNTVHRFQSD
     LRELTLWSTK VEGSAPSILL IDETKSDFAN RRRVVICLFD LQAEIDAHQH VYESVSGTGA
     QIVHSMQQQQ DIAGQAEDAV SLQKCLEDMN HRWTRLKAKS VEIRGRLEAN AEQWNQLLET
     LENLTRWTTE RETEIERQQP VGGDVHSIRQ QHLDHQAIRT QLEEKRASVE QSLETGRLYL
     REEGLEDKRL KSEGSGSEKS PEQEARSIIK KIRRYVRLLN RKWVELNQRS NEWQHCIDET
     LEKMEVFHTT LAEMTEDLTE AERERSKWLR VGDVVLDNLK KEIQSTNAFQ QNRVLPLRAQ
     CDQLNDMANQ FHEMRVVLSH KNVSRLEDLS NRLKTLLASV EDRMQHLQEA LRDFGPNSQH
     LLSASIEHPF ERAVAVNKVP YFINHDTETT HWDHPEMTKL MAGIADLNEV RFSAYRTAMK
     LRTVQKKLCL DLLSMTSATE AFERHQLNSG GDKTMDVMQI INCTLEMYEA LAEMHPTLVN
     VPLCVDLVLN WLLNVYDSIR NGHIRVLSFK ICIILMCKAH LEDKYRYLFT ELADAKGGMD
     QRQLGLLLHD CLQLPRQMGE IASFGGSNIE PSVRSCFAKA HKEESLEVHE LLDWLKMEPQ
     SMVWVPVLHR LAAAETAKHQ AKCNICKEFP IVGFRYRCLR CFNFDMCQNC FFSGRKAKGH
     KLTHPMQEYC TATTSGEDVR DFTKMFKNKF RSKRYFKKHP RMGYLPVDSV HEGDPIECPA
     APQSSPQHNS STLEMHSRLE LYANRLAEVE QRQCSATPDS DDEHQLIAQY CMSLQGDTPS
     HQVSSPLQIM MGIDMDQRAE LEAMINDLEE ENLHLQKEYG RLKQVQLHQL EEEDGHFDEI
     AQVASSVLPQ QQNGDADVAG GDAEMLAEAK LLRQHKGRLE ARMQILEDHN RQLEAQLQRL
     RQLLDQPDSG PRIVTMVSSS ATTPGMSAAS SQSSLPYPGM HVSSYQSSTA GSGSYINGHS
     ELRASSAEGP PSSMSTSAPA YPGCSQHPVH QSLQQKARHL QQITVRHEPL RDPDDDDYRE
     GGTATDEELE EVMREIEHSF PPEPAVSKGS SANVGDLFRM AGQVGTAVST LVTVMTDEEL
     SDEEEDEVDE DERK
//
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