ID A0A3Q1ELG8_9TELE Unreviewed; 2342 AA.
AC A0A3Q1ELG8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000004212.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000004212.1}
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; 80966.ENSAPOP00000004212; -.
DR Ensembl; ENSAPOT00000010437.1; ENSAPOP00000004212.1; ENSAPOG00000005935.1.
DR GeneTree; ENSGT00940000154864; -.
DR InParanoid; A0A3Q1ELG8; -.
DR Proteomes; UP000257200; 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; cd21317; CH_SPTBN2_rpt1; 1.
DR CDD; cd21321; CH_SPTBN2_rpt2; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.20.58.60; -; 13.
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:SF325; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 57..161
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 176..281
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2177..2287
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2088..2178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1032
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1097..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1236..1274
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1422..1449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1852..1879
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1977..2004
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2108..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2321..2335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2342 AA; 268484 MW; C899B9AA16BB7ED7 CRC64;
MSTISPTDFD SLEIQQQYND INNRWDLAAE TDWDNENSSA RLFERSRIKA LADEREAVQK
KTFTKWVNSH LGRVTCRIGD LYTDLRDGRM LIRLLEVLSG EQLPKPTKGR MRIHCLENVD
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLIWTIILRF QIQDISVETE DNKEKKSAKD
ALLLWCQMKT AGYPNVNIHN FTTSWRDGLA FNAIVHKHRP DLIEFDNLKR SNAHYNLQNA
FNVAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDYA
IEADQLIEKY ETLASELLQW IEQTIVTLND RQLANSLSAV QNQLQAFNSY RTVEKPPKFT
EKGNLEVLLF TIQSKMRANN QKVYMPREGK LISDINKAWE RLEKAEHERE LALRNELIRQ
EKLEMLAARF DRKAAMRETW LSENQRLVSQ DNFGTDLGAV EAATRKHEAI ETDIGAYWER
VAAVEAVAKE LEAEGYHDVR RILARRDNVL RLWEYLKELL AARRERLNAH RDLQRLFQEM
RYIMDWMADE KGRLQSQDSG KHLHDVLDLL QKHTLVEADI SAQAERIKAV QGAAKRFTSY
EQAYKPCEPG LVSEKVDLLG QAYEELGQLA GQRRECLEDS RRLWQFMWDV GEEAAWIREQ
EQILASGDCG RDLTSALHLL SKHEAFRDEM AARYGPLNNS IAAGEALVQE GHFGAPQVTE
RIQDIRAQWT HLEELREQNL KEAVALNQFQ TDANDMEAWI METLRQVSSQ EVGHDEFSTQ
TLARKQREIE EEIQSHHPLI DSLQEQAQAL PQAYIGFPQV EGRLPAIEQR YEELESLSAA
RRQALEGALA LYRMFSEAGA CQLWVEEKEQ WLHGMEIPTK LEDLEVVQQR FETLEPEMNN
VGARVTDVNQ VAEQLLSSDN CNKDQIHQTK DQLNNRWKEF EQLSGQKKQA LESALNIQNY
HLECNEIQTW MKEKTKVIES TQSLGNDLAG VMALQRKLTG MERDLEAIQG KLDDLRNEAE
KLAKEHPDQA GEIQGRLAEI QEVWEELNAT MKRREESLGE ASKLQGFLRD LDDFQSWLSR
TQTAVASEDI PTSLPEAESL LAQHESIKNE VDNYKDDYEK MRAVGEEVTQ GQTDAQHMFL
AQRLQALDTG WHELRRMWEN RHSLLAQAFD FQTFLRDAKQ AEAFLNSQEY VLSHTEMPTS
LQAAEEAIKK HEDFLTTTEA SEEKITGVVE AGRRLINDSN ANSDKIQEKV DSIQERHLKN
KEAANELLAK LKDNRELQHF LQDGQELTLW INEKMLTAQD MSYDEARNLH SKWQKHQAFM
AELASNKDWL DKIDKEGQAL VAEKPELKPV VQQTLEDLQR QWEELEGTTQ TKAQCLFDAN
RAELFTQSCS ALDVWLKNLE GQLHSDDYGK DLTSVNILLK KHQMLEHQME VREKEVQSLQ
SQALALTQED AGLAEVDGQQ RRVTDNFSNL QDPLKLRRQR LLASKEAHQF NRDLEDEILW
VKERMPLATS TDHGKDLPTV QLLIKKNQTL QKEIQGHQPR IDDIHRRGKT QSQVDGERQS
VLEERLVELK DLWDQLIAET DKRHARLIEA NRAQQFYADA AEAEAWMGEQ ELHMMSEEKA
KDEQSALVMV KKHQSLEQAL EDYAQTIHQL ANSSRLMVTS EHPESERITL RQAQVDKLYA
GLKDLAEERR GRLQERLRLT QLKREVDDLE QWIAEREVVA GSHELGQDYE HVTMLRDKFR
EFARDTSMIG QERVDGVNGL ADDLIESGHP ENASVAEWKD GLNEAWADLL ELIDTRTQML
AASYELHRFH QDAMEVLGRV KEKREALPSD LGRDLNTVQH LHRQHNTFEH DIQALSGQVN
QVQDDAARLQ KAYAGEKADD IHRSEHAVTS AWEGLLEAGQ ARRLLLLDTV EKFRFFNMVR
DLMLWMDGVN LQIDAHDSPR DVSSAGLVIA NHQDIKSEIE TRADSFTACT EMGNTLINNN
HYAADEVQEK LAQLQEKRDK INKKWQDKMD HLQIVLEVLQ FGRDAYVAES WLAGQEPLVR
AAELGSNVDE VESLIKRHEA FEKLAAAWEE RFVSLEKLTT LEEYEIQRRR EEEERARRPP
TPPPVEEVAQ SETESQAHDS AASRVLSSSS PPFMSWCELQ GSESESVNGP GRDSGLASSR
LEPSATLPSR GGAESGPEAM EGMLCRKQEM ESHSKKAASR SWQNVYCVLR KGSLGFYKDS
KSASNGIPYH GEVPISLGEA VCEVAHDYKK RKHVFKLRLG DGKEYLFQAK DEAEMSSWIR
SILGSIPSGA GDSPGGPRAL SRAMTMPPIS PSSADAGGVT MRNKEGKEKD REKRFSFFGK
KK
//
