ID A0A484B175_DRONA Unreviewed; 2309 AA.
AC A0A484B175;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN ORFNames=AWZ03_011065 {ECO:0000313|EMBL:TDG42516.1};
OS Drosophila navojoa (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG42516.1, ECO:0000313|Proteomes:UP000295192};
RN [1] {ECO:0000313|EMBL:TDG42516.1, ECO:0000313|Proteomes:UP000295192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG42516.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:TDG42516.1};
RX PubMed=30423125; DOI=.1093/jhered/esy059;
RA Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT the mojavensis Cluster.";
RL J. Hered. 110:118-123(2019).
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDG42516.1}.
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DR EMBL; LSRL02000225; TDG42516.1; -; Genomic_DNA.
DR RefSeq; XP_017964205.1; XM_018108716.1.
DR STRING; 7232.A0A484B175; -.
DR GeneID; 108656578; -.
DR KEGG; dnv:108656578; -.
DR OMA; DNHEPWI; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000295192; 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 GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; -; 10.
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; 17.
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; 15.
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:UP000295192};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 50..154
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 169..274
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2165..2277
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2096..2128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2154..2184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2283..2309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1281..1343
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1628..1655
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2170..2184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2309 AA; 267408 MW; 00EF0C7ECB1D26BC CRC64;
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV
NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR
EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ
MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK
LGLAKLLDAE DVCVDHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMI
HDYEHFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV
LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA
ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV
CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM
EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSEDPESYKP
CDPEIIVSRV QQLEDAYAEL VRRAVERRSH LEESRKLWQF YWDTADEENW IKEKEQIVST
DEIGHDLTTV NLLLSKHKAL ESEITSHDPQ LQNVAKVGAE LITEGHLGAD RIKDRLKEIL
SKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL
KKHKDVADEL KNYAEVIDAL HKQAETLKLN EPEKANVDKR LEAIDTRYKE LTELAKLRKQ
RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMVPGKDIED VEIMKHRFEG FDKEMNANAS
RVAVVNQLAR QLLHVEHPNS DEILDRQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE
CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLGREADSIE
VEHPEEAQLI RNRIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT
DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKSMME YGERLTSEGN TSEDPQYMFL
RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKEH FDAEKIGKRA ENITGRRDDN
RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYVTSQD ETYRSAKTIH SKWTRHQAFE
AEIAANKERL YEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGALLFDAN
REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID
KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KQLEKKKEAF QFCRDVEDEK
LWINEKLPVA NSTDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED
AKKFEALISD LTAKWQELKD AIENRKRHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED
RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS SDDVSSGDAV AVKQSQLDKL
YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD YDHVTLLSER
FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLTTLYSQ
VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARRQKLAD TGDLFRFFNM
VRILTIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFSA CISLGKELLT
RNHYASADIK DRLKQLNNSR NALLLRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY
LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQEKAEEAER
QRIKEEQEAK AASEAAELAK REAERRDDVD VAAGAHDEAA AADTAVDTER VIETQTERGA
TPAAGDGQEG YVTRKHEWES ATKKASNRSW DKVYMAARSG RVSFFKDQKG CKSNPELTFR
GEPSYDLQGA VIEIASDYTK KKHVLRVKLA SGAEFLLQAH DDTEMSQWVS ALKAQSESAA
VAASRSQTLP ATSQKDEPKR RSFFTLKKK
//
