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Database: UniProt
Entry: H2ZPE1_CIOSA
LinkDB: H2ZPE1_CIOSA
Original site: H2ZPE1_CIOSA 
ID   H2ZPE1_CIOSA            Unreviewed;      2309 AA.
AC   H2ZPE1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000019457.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000019457.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR   Ensembl; ENSCSAVT00000019667.1; ENSCSAVP00000019457.1; ENSCSAVG00000011411.1.
DR   GeneTree; ENSGT00940000154864; -.
DR   Proteomes; UP000007875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR   CDD; cd21246; CH_SPTB-like_rpt1; 1.
DR   CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 9.
DR   Gene3D; 1.20.58.60; -; 14.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF447; SPECTRIN BETA CHAIN; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF00435; Spectrin; 16.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 14.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467,
KW   ECO:0000256|PIRNR:PIRNR002297};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|PIRNR:PIRNR002297}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002297};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR002297};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          8..112
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          127..232
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2192..2302
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2043..2077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2121..2174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          411..445
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          947..988
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1053..1080
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1383..1410
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2150..2164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2309 AA;  266114 MW;  1A1A5764C9464B8F CRC64;
     SILDEREAVQ KKTFTKWVNS HLVRVSCRIQ DLYMDLRDGR SLIKLLEILS GERLPKPTRG
     KMRIHCLENT GKALQFLKSK KVHLENMGPH DIVDGNHRLI LGLIWTIILR FQIQDISVET
     EDNRETRSAK DALLLWCQMK TAGYANVNVH NFNTSWRDGL AFNAIIHKHR PDLIDYDSLK
     KSNAMHNLQN AFNVAEQQLG LTKLLDPEDI VVERPDEKSI ITYVVTYYHY FSKMKAIAVE
     GKRIGKVLDS ALESNQMVEK YDSLASDLLD WIEQTIEILN DRTFANSLSG VSAQLAAFNN
     YRTAEKPQKF QEKGNLEVLL FTLQSKMRAN NQKPYLPKEG KLVSDINKAW EKLEKAEHGR
     ELAIRNELIR QERLELLASR FDRKAAMRET WLSENQKLVT QDNFGGDLPA VEAATKKHEA
     IETDVKAYEE RVQAVVDVAS ELQREDYHDI TRVNQRKDNV LQLWEYLLEL LQGRRTRLEL
     NVRLQQMFEE MMSLLDWMDD MKGQLANEDL GQHLMGVEDI LQKHMLLEQD ITVHGDRVKA
     IESQSQEFLQ PTNDYSACEP SAVEDKVVGV RTTYDQLCKQ AADRRAKLDE SRRMHLFFAT
     MAEEVAWVKE KEQLLNSDDL GRDLTSVHSL LTKQKALEDE MNGRKAMLAN AIAVGEDLIS
     EDHFASQDIA KHISDINEQW KNLEELAEAR NELLRANKLY QFYADTDDVD TWLVDMFRIV
     STDDCGRDEP SVLSLLKKHA QVQEELTKYE GVIKALHDEA DGLTEKDRES VEVQERLRSV
     DSRYKELLDF AKLRKEKLID ARALYKFYGE ADTISAWIAE KEQVLENMLV PDNIEDMELV
     QHRFEGYENE VNKLAPQVAV VNQMARGLVQ TQHPNSDDVS AKQNELNARW NALRALLEER
     REILASAKGL HGFKLECDET EGWIKDKARV LAAGAEDQLS DRDLAGVVAL QRKLSSMELD
     LAAIQAKLDN LRDEADRLSN EHPEEADEIR KKFEQMERVW QELRDMLRQR EDSLGEAGNL
     QKFLRDLDRF QAWLSTTQTT IASEDMPQSL PEAEKLLQQH QAIKLEIDNY QADYEEIKST
     GAQVTSGRED EPQYMFLGQR LQALDQGWIE LHKMWENRNH FLNEAKEYQA FIRDCKQAEQ
     ILTNQEYALE SARRSSAAAS TPDSAEEVMK KHEAFVATMA SADERVEAVL RDAGKLADAD
     HHAADKIKER AEKIAERRAK NKEEAGEVST MLRDNLALQK FVADCDELSE WVNEKMLTAK
     DATYDDARNL HSKWQKHQAF SAELTANKDR LERLEEDGST LAKSKPEWKD QIDVRLDDLR
     KHWEALESCT KTKEKTLFEA NKAELFSQTC EDLEKFASMM EEQLNSDDVG KDLASVNVLL
     KDHLAQQDEI EVRKQEVQEL ESQAAVLRSE GDEDVDTMNE ERAKIKHRIE DLDEPLTKRK
     DALENSKQLH QFYRDVQDEK LWIDEKHPQA TSNELGNSLQ EVQALQKKHQ ALRSELTAHE
     PVVVAVCHRG VAMATEDNPN TDKINEKCHE LQENWNRLLE DVDERKRKLS EAENAQQYFF
     DADEAVVLME EQELYMMSDE KAKDSQGATK MLKKHQAQEQ NIDDFADTIQ QLSKTCRDLC
     EQEHPQSEQL STRQQQVDQT YAGLKDLAEE RRMKLRERCD LFRLSRDIDD LEQWIAQREV
     VAASQEQGQD FDHVSMLQDQ FNDFQRDTIK TGEERVADAM RMSDELINAG HTDAQDIAGW
     KDTIRDAWAD LLELIDTRVE MLAAAYALHK FHYDAAEILA RIQEKRQEVP EELGRDHDAV
     ENFKREHDIF AQDIKAIGAQ VEAITSAGSE LEGRYAGDDL QEIQKKIEAV LSAWNNLLSL
     VKKRAALLSD ALNKFRFFNM CRDLMDWMES TVRQIDLQEK PRDVSGVETA MSLHQGTKAE
     IDARNGSFEE CTQLGQHLIT TGHYASDEIR VKLDELGAKR NHVVDRWQEK WELNLLMEVY
     QFAHDANTCD AWVQQQLGLI RDMPVDTCRS ADDADQLLRR LDGFEKAAVP WEDRFAALEK
     LTEVSQEEQE KKRKEEEEQE ERRRKAEEDE QKIKKEAELE AARPVSLALS PEDLWLPRNE
     NSVMYSGLCL DSSEALKLLR KQGRTKPPLK PKRSNGDVGN LMRSQAHSLR MKMYENRRNR
     RPSPIPTKDQ GNARRIQLFP QTKAPQDSES PDVPYQGFLK RKSTMFSPSK KAPNRSWNSV
     FCVLQDKNLA FYKDPKAASQ RASFHGEQSI SLENATIEIA SDYKKRKNVL RLRLSAGMEY
     LFQAKDEEEL NVWLNRLQSQ NLNASIGSG
//
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