ID H3DNS4_TETNG Unreviewed; 2496 AA.
AC H3DNS4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000022173.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000022173.1}
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 STRING; 99883.ENSTNIP00000022173; -.
DR Ensembl; ENSTNIT00000022411.1; ENSTNIP00000022173.1; ENSTNIG00000018985.1.
DR GeneTree; ENSGT00940000156343; -.
DR HOGENOM; CLU_000146_0_1_1; -.
DR InParanoid; H3DNS4; -.
DR OMA; ENQMEDW; -.
DR TreeFam; TF313446; -.
DR Proteomes; UP000007303; 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; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.58.60; -; 12.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
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:SF232; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 4; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00435; Spectrin; 15.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 5.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00150; SPEC; 15.
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; 1.
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:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 53..157
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2354..2462
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2208..2272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2462..2496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1078..1112
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1363..1416
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1501..1528
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2225..2262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2496 AA; 287040 MW; D33EFB1EE3C27779 CRC64;
MANASSDLDN AEAQRQLNNN NRPIGSGFWE TECTSSKLFE CSRIKALADE RDAVQKKTFT
KWVNSHLSRV SCRISDLYND LRDGYMLTRL LEVLSGELLP RPTRGRMRIH CLENVDKALQ
FLKEQRVHLE NVGSHDIVDG NHRLTLGLIW TIILRFQVER NRNHTQKHMM TRKASNVLCQ
GNRMLADVTT RAPNKHLKCY FQGRLSELPH HHSAITHSVC WTKPKCHLRP SSLRVACAFC
FALQQGHTLT HAPRPISLRT HKHGEAHMHR TRISTCAPQF QAPAALTQKY KKRKSKCHVS
VTPQWYLCSH TLYTISIFLL KCSQCSVYCS KLHMLSMSTF VQIQVIKIET EDNRETRSAL
VPDEDSRVSD VNYTWEFHQY TSVSMNPFKA SDIRRSTSKI SPLAFDHKTT MRQAWLNENQ
RLVSQDNFGY DLPAVEAAMK KHEAIEADIA SYEERIGVVV ELSAEMEAEA YYDIRRILAR
KENILGQWKL LKELVAGRRT RLEKNLSLQK IFQDMVYMID WMEDTQVQLL SKDYGKHLLE
VEDLLQKHSL QEADIAVQAE RVESLNKAAL KFTTIQGYQP CDPQVICNRV NHVSSCLEEL
KQLASKRCTD LEESRQLWAF LQELEESDAW IREKSSILGA QGFGKDLTSV LKLLQKHKTL
AGELLAHRSL LQNTIKQGKQ ILSEKSFGTT GIQEHILELK NQWKRLEDQA GQRLGHLQEA
LNFFQFSTEM DDLVAWLQDA YRLVSSEDFG HDEYSTQSLL KKHAEFLVFL VFARLERRDE
GPNCGGQEGR FPPSNQVLDN CIEAEKIIDR YEALASDLLD WIEKTIAVIS NQKEAHQATI
LCALWLIHEK GNLEVLLFTI QSKLRANNQK PYVPHDGKLI SDINKVIHPS ICVHYXLKPK
RSDSDHIKFC AVFSLPRWNS IVELVEQKKN QLNSMLRLQN YLLECVEIKS QIQDKRKAID
STQYMGSDLG GVMALQRRLS TMEGALSVLE PKLLHLQEEA ENLATAHPSR AMEVLVPFDD
ISVEWEELKH TLQGCEDSLM VASRLQSFIQ DLDSFLTWLV QTQTVAASDQ LPNDLEEAET
LINKHAALKE EIGRYEEDYE RLQSMNELLD SDEAPLPQAA LQQWLQKLDV GWNKLLEMWE
SRREVLVQAH IFHLFLRDVK QAESLLNNQE SALAHVELPT TVETVEAAIK KHKDFTTSME
LNLHRIKAVI EAGESLISQN NIYSERIRER IDTLANRGNQ NREMAQKWLE KLNHQWELQR
FLQNCHELGD WVYEKMLMAR DGSRDESQKL HKKWLKHQAF MAELAQNKDW LDKIEKEGQQ
LMQEKPELSP VVRRKLEEIR DCWQDLESTT QAKARQLFEA NKADLVVQSY ESLDQRLNQL
EDQLAYVDQG QDLTGVNNQL KKLQTMENQM EDWYKEVGLL QVQAATIPQQ TQRNETVSER
QTAVEARMVR LIEPLKERRR ILLASKELHQ VRRDLEDEIL WIQERLPMAM SQEHGSTLQE
VQQLMKKNQM LQRELQGHKG RIEDVLERAG IIASIRSPEA DSVRTGHDQL AQLWNLLWVE
TERRQLVLDA MYQAQQYFFD TAEVEAWLSE QELHMMNEEK GKDEPSTLQL LKKHLVLEQT
IEDYAETIGL LSQQCRQLLE MGHPDCEHIS RRQSQIDRLY VSLKDLVEER KSRLEQQYWL
YQLNREVDEL EQWIAQKEVV ASSPELGQDF EHVTVLQDKF TKFATETGSV GQERVTAVNQ
MVDELIDYGH SEAATIAEWK DGVNEAWADL LELMETRSQM LAASHQLHKF FSDCREILAQ
IDDKHRRLPE VRAKQGNSAN TNTLKRLLHS FEQDIQLLVT QVRHLQESAA QLRTVYAGEK
AEAIACCEHE VMQSWKELLT SCEECRVEIT TETDKLKFLG MVRDQLIWMD SIICQIGTGE
KPRDVSSVEV LMNYHQSLKS EVEARSRSTL ECIEMGKTLL AVRNPAAEEI KEKLEKVVAK
QHELSEKWDK HWEVLQQLLE VHQFAQEAVV AEAWLTAQEP LVNSSLLGES VDEVEQLIRR
HEAFRKAAAT WEERFSSLRR LTTVEKLKAE QGKLPPTPLL GRKVFLDPQD AIPSPATLPR
LPVSPVARQT MLGSTVASYT PVMNGSGYRH TLEPRHAGAG VVGVAAGLGQ PSPSSIASVA
TAAMLVSANQ MRERANTIKE QATKAVEQLI QARRDELPQE VWREHAERRE RRTLERQTSS
EQEGHGGLDV RRRERDRHRL ERQESSEHDT GHSDRRSAGG ERRSTMAEIV EQVQEREAAQ
VCMPCSALQA RGEVPRLPNG FPEKSSRPDR PRARDRPKPR RRPRPREAGD TTARRSRSAP
AQSSPAVPQP PTHTAHHEGF LFRKLDIESL KKSTNSRSWV NLYCVLNKGE IGFYKDAKNT
STPYNNEPLL SLSHCHCDIT NGYKKKKNVF TLKTKDGSEF LFHAKDEEDL KAWVNNITTS
ISEHEEIAKR GQPQPTTSST DEGTRREGSK ADNRSE
//
