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Database: UniProt
Entry: A0A3Q3FYM9_9LABR
LinkDB: A0A3Q3FYM9_9LABR
Original site: A0A3Q3FYM9_9LABR 
ID   A0A3Q3FYM9_9LABR        Unreviewed;      2277 AA.
AC   A0A3Q3FYM9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=SPTBN1 {ECO:0000313|Ensembl:ENSLBEP00000024504.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000024504.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000024504.1}
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; ENSLBET00000025766.1; ENSLBEP00000024504.1; ENSLBEG00000018090.1.
DR   GeneTree; ENSGT00940000154864; -.
DR   Proteomes; UP000261660; 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: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; 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; 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; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 13.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
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|PIRNR:PIRNR002297};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          34..138
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          150..238
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          2074..2141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2224..2277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          952..986
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1058..1085
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2076..2104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2111..2127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2224..2253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2254..2270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2277 AA;  262792 MW;  6C5EFBB6D9590F59 CRC64;
     MMEAEWAMGD PVHQQQNYNL LEGRFKQLQD EREAVQKKTF TKWINSHLSR VSCRITDLYM
     DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD
     GNHRLTLGLI WTIILRFQIQ DIRFCSVVMY PNVNIHNFST SWRDGMAFNA LIHKHRPDLI
     DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL LDPEDISVDH PDEKSVITYV VTYYHYFSKM
     KALKVEGKRI GKVLDNAIET EKMVEKYESL ASDLLEWIEQ TIIILNNRKF ANSLLGVQQQ
     LQAFNTYRTV EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE
     KAEHERELAL RTELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLQAVEAA
     TKKHEAIETD ITAYEERVQA VVSVARELEV EHYHDIKRVT ARKDNVIRLW EYLLELLKAR
     RQRLEMNLGL QRVFQEMLYI MDWMDEMKML LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ
     ADRVKAVSTN ANKYSVNDDG YKPCDPMVIQ DRVSHLEFCY QELTQLAAER RARLEESRRL
     WKFFWEMAEE EGWIREKEQI LSSVEHGKDL TGALRLLSQQ RALEDEMSGR AGHLQHSVAE
     GEAMVEAGHF AAAKIQDRIA DLKAQWAGLE QLAAVRKTRL EEALALHQFQ ADADDVDAWT
     LDALRIVSSG ETGHDEFSTQ ALVRKHKDAA AEVASYRPVI DSLHEQAAAL PKEEAESEEV
     RGRLAGIEER YREVSELTKL RKQALQDALA LYKMFSEANA CEVWIDEKEQ WLNSMEIPEK
     LEDLEVVQHR YDTPLEPEMN NQASRVAVVN QIARQLMHNG HPSEREIKSQ QDKLNNRWSQ
     FRDLVDLKKE SLNSALGVQN YHLDCNETKS WIKEKTKVIE STQELGNDLT GVMALQRKLT
     GMERDLAAIE DKLGDLRGEA ERLAQEHPDQ AKAITGRLSE ITAVWEEMKN TLKNREDSLG
     EARKLQQFLR ELDDFQSWLS RTQTAIASED MPNTLAEAEK LMAQHEGIKN EIQNYEEDYQ
     KMRDMGEMVT QGQTDAQYMF LRQRLQALDT GWNELHKMWE NRQNLLSQSH AYQLFLRDTK
     QAEAFLNNQE YVLAHTEMPT TLEAAEAAIK KQEDFMTTMD ANEDKINGVV EAGRRLASDG
     NINAEKIQER VASIDDRHKK NREAAVELLM RLKDNRDLQK FLQDCQELSL WINEKMLTAQ
     DMTYDEARNL HSKWLKHQAF MAELQSNKEW LDKIQKDGTL LVSEKPETDA VVKEKLSALH
     AMWAELESTT QTKAQCLFDA NKAELFTQSC ADLDKWMGGL EGQIQSDDYG KDLTSVNILL
     KKQQMLEKQV EVRQRGVELQ SQVKALGQEV KDTEEVDGRR QLVENKFQEL LDPLRRRRNF
     LVASREVHQF NRDLEDEILW VQERMPVATS TDHGNNLQTV QLLIKKNQTL QKEIQGHQPR
     INDLLEHSAS LLQDESLSGE VIRQRLADLQ ELWRREAHKA QQYYFDAAEA EAWMSEQELY
     MMSEEKAKDE LSAVTMQKKH QIVEQAVEDY AETSTCCPRP AERISMRQSQ VDKLYAGLKD
     LSEERRGKLD ERLRLFQLNR EVDDLEQWIA EREVVAGSHE LGQDYEHVTM LQERFREFAR
     DTGNIGQERV DAVNRLADEL INTGHGDAAT VAEWKDGLNE AWADLLELID TRTQILAASF
     ELHKFYHDAK EILGRIVDKQ KKLPEEVGRD QNTVDTLQRM HTTFEHDIQA LGTQVRQLQE
     DAVRLQSAYA GDKADDIQRR ESEVLEAWRI LLEACEGRRL RLLDTGDKFR FFSMVRDLML
     WMEDVIRLIE AQENPRDVSS VELLMNNHQG IKAEIDARND SFTACIELGK ALLARKHYAS
     EEIKEKLLQL TDKRKDMIDK WEDRWEWLRL ILEVHQFSRD AGVAEAWLLG QEPYLSGRDM
     GQSVDEVEKL IKRHEAFEKS AATWEERFSA LERLTTVRGS RRRRSFLRKP PTPELLPVQE
     SFKIHHVRLE QMSLCIPPSQ DGMVDGELVN GVVERSSKEP SPSGSPTSGR KSKTSQSSTL
     PPGTRSPRPR WRASCTANTS GRGTTRRPPT GNKDPLLQEG ETSHSACTAL ITLSPPSLIG
     RSWHNVYCVI NNQEMGFYKD SKAASQGVPY HNEVPVGLKE ATCSGFREEM STWIQAILNA
     GADRSSVQGS HPGTPVSGRA QTLPATVTLT TESSPGKREK DKEKEKEKRF SLFKKKQ
//
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