ID A0A3B3QCW7_9TELE Unreviewed; 2361 AA.
AC A0A3B3QCW7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSPKIP00000003998.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000003998.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000003998.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 1676925.ENSPKIP00000003998; -.
DR Ensembl; ENSPKIT00000027970.1; ENSPKIP00000003998.1; ENSPKIG00000021235.1.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000261540; Unplaced.
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; -; 12.
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:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 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; 13.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 58..162
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 177..282
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2186..2296
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2093..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2298..2361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..495
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 995..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1098..1128
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1426..1453
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2116..2133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2298..2329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2330..2354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2361 AA; 273208 MW; 8E02179CA55226CD CRC64;
MPCAGTLGVS RRWRCHLSAP RNQCGSLSLR RLSLQPPHSA PHRGLRLAVR RSTDEREAVQ
KKTFTKWVNS HLARVSCRIT DLYMDLRDGR MLIKLLEVLS GERLPKPTKG RMRIHCLENV
DKALQFLKEQ RVHLENMGSH DIVDGNHRLT LGLIWTIILR FQIQDISVET EDNKEKKSAK
DALLLWCQMK TAGYPNVNIH NFTTSWRDGM AFNALIHKHR PDLIDFDKLK KSNAHYNLQN
AFNLAEQHLG LTKLLDPEDI SVDHPDEKSI ITYVVTYYHY FSKMKALKVE GKRIGKVLDN
AIETEKMIEK YESLASDLLE WIEQTIIILN NRKFANSLVG VQQQLQAFNT YRTVEKPPKF
TEKGNLEVLL FTIQSKMRAN NQKVYMPREG KLISDINKAW ERLEKAEHER ELALRTELIR
QEKLEQLARR FDRKAAMRET WLSENQRLVS QDNFGFDLQA VEAATKKHEA IETDIAAYEE
RVQAVVAVAR ELEAENYHDI KRITARKDNV IRLWEYLLEL LRARRSRLEM NLGLQKVFQE
MLYIMDWMDE MKMLLLSQDY GKHLLGVEDL LQKHALVEAD IGIQADRVKN VNANAQKFAL
DTEGYKPCDP QVIRDRVAHM EFCYQELTQL AAERRARLEE SRRLWKFFWE MAEEEGWMRE
KEQILSSEDC GKDLTAAIRL LSKHRAFEDE MSGRSGRLQQ SVREGEAMVE AQHFGSDKIR
ERTTDIREQW AALGRLAAVR RTRLEEALSL HQFQVDADDI DTWMLDVLRI VSSADVGHDE
FSTQALVKKH KDVAEETASY RPIIDALREQ SCALPGEHGQ SEEVQSRLAG IEERYREVAE
LTRLRKQALQ DALALYKMSS EADACELWID EKEQWLNSMQ IPEKLEDLEV IQHRFESLEP
EMNNQASRVA VVNQIARQLV HSGHPGEKEI KAQQDKLNTR WSQFRDLVDL KKDALNSALG
VQNYHLECNE TKSWIREKTK VIESTQELGN DLAGVMALQR KLTGMERDLV AIEDKLTDLQ
KEAERLAAEH PDQAQAIMGR LAEITGVWEE MKTTLRNREE SLGEASKLQQ FLRDLDDFQS
WLSRTQTAIA SEDMPNTLAE AEKLLTQHEN IKNEINNYEE DYQKMRDMGE MVTQGQTDAQ
YMFLRQRLQA LDTGWNELHK MWENRQSLLS QSHAYQLFLR DTKQAEAFLN NQEYVLAHTE
MPTTLEAAEG AIKKQEDFMT TMDANEEKIN AVVETGRRLV SDGNINSERI QERVDSIDDR
HKKNREAASE LLMRLKDNRD LQKFLQDCQE LSLWINEKML TAQDMSYDEA RNLHSKWLKH
QAFMAELQSN KEWLDKIEKD GTQLVAEKPE TQAVVKEKLS SLHSMWNDLE STTQTKAQCL
FDANKAELFS QSCADLDKWL VGLDGQIHSD DYGKDLTSVN ILLKKQQMLE NQVEVRRKEV
EELQSQAQAL SQEGKDSDEV DGRRRGVEHK FQKMLDPLHK RKDNLMASKE IHQFNRDVED
EILWVEERMP LATSTDHGHN LQTVQLLIKK NQTLQKEVQG HQPRFNDIFE RSQSILKDDS
PTAEAIRQRL ADLRQLWDQM IQETENRHSR LEEAHKAQQY YFDAAEAEAW MSEQELYMMS
EEKAKDEQSA VAMLKKHQIL EQAVEDYAET VHQLSKTSRA LVAAGHPESE RINMRQSQVD
KLYAGLKDLS EERRGKLDER FRLFQLNREV DDLEQWIAER EVVAGSHELG QDYEHVTMLQ
ERFREFARDT GNIGQERVDA VNQMADDLIN SGHSDAATIA EWKDGLNEAW ADLLELIDTR
TQILAASFEL HKFYHDAKEI LGRILDKHKK LPEELGRDQN TVETLQRMHT TFEHDIQALG
TQVRQLQEDA VRLQSAYAGD KADDIQKRES EVLETWKSLL EACEGRRVRL LDTGDKFRFF
SMVRDLMLWM EDVIRLIEAQ EKPRDVSSVE LLMNNHQGIK AEIDARNDSF TTCIELGKAL
LARKHYASDE IKEKLVQLTD KRKDMIDKWE DRWEWLRLVL EVHQFSRDAG VAETWLLAQE
PYLSSREMGQ SVDEVEKLIK RHEAFEKSAA TWEERFSALE RLTTMELLEV RRQQEEEERR
RQPLSPEALP APDSDSQQRE GEQASQNGLP SDQDSPRDGV DGADMVNGVA ERSSKEPSPA
PSPSAERKGR SSQAATLPAK AQDSPSAQLE GFLHRKHEWE AHNKKASSRS WHNVYCVINN
QEMGFYKDSK TASQGIPYHS EIPISLKDAV CEVALDYKKK KHVFKLRISD GNEYLFQAKD
DEEMNTWIQA ITSAVTSAAT SDVTPSSQST PASSRAQTLP TGVSLTTESS PGKKEKEKDK
EKEKEKEKEK EKRFSLFSKK K
//
