ID L5M5M5_MYODS Unreviewed; 2334 AA.
AC L5M5M5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN ORFNames=MDA_GLEAN10010926 {ECO:0000313|EMBL:ELK32988.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32988.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR EMBL; KB104801; ELK32988.1; -; Genomic_DNA.
DR eggNOG; KOG0517; Eukaryota.
DR Proteomes; UP000010556; 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; cd21319; CH_SPTB_rpt2; 1.
DR CDD; cd21317; CH_SPTBN2_rpt1; 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:SF248; SPECTRIN BETA CHAIN, ERYTHROCYTIC; 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:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 54..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 175..280
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2184..2294
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2077..2183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2312..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 459..500
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2101..2124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2144..2158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2334 AA; 268249 MW; 38484F110825EED7 CRC64;
MTSATEFENV ANQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF
TKWVNSHLAR KSCRITDLYK DLRDGQMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVVPEGPE GRETRSAKDA
LLLWCQMKTA GYPHVNVTNF TSSWKDGLAF NALIHKHRPD LIDFDKLKDS NARHNLEHAF
DVAERQLGII PLLDPEDVFT ENPDEKSIIT YVVAFYHYFS KMKVLAVEGK RIGKVIDHAI
ETEKMIEKYS GLASDLLTWI EQTITILNSR KFANSLTGVQ QQLQAFSTYR TVEKPPKFQE
KGNLEVLLFT IQSRMRANNQ KVYTPHDGKL VSDINRAWES LEEAEYRREL ALRNELIRQE
KLEQLARRFD RKAAMRETWL NENQRLVAQD NFGYDLAAVE AAKKKHEAIE TDTAAYEERV
RALEDLAQEL EKENYHDQKR ITARKDNILR LWSYLQELLA SRRQRLETTL ALQKLFQDML
HSIDWMDEIK AHLLSAEFGK HLLEVEDLLQ KHKLMEADIA IQGDKVKAIN TATLQFTEGK
GYQPCDPQVI QDRVSHLEQC FEELSNMAAG RKAQLEQSKR LWKFFWEMDE AESWIKEKEQ
IYSSLDYGKD LTSVLILQRK HKAFEDELRG LDAHLDQIFQ EAEGMVARKQ FGHPQIEARI
KEVSAQWAQL KELAAFRKKN LQDAENFFQF QGDADDLKAW LQDAHKLLTG EDVGQDEGAT
RALGKKHKDF LEELEESRAV MEHLERQAQS FPQEFRDSPD VTNRLQALRD LYQQVVAQAD
LRRQKLQEAL DLYTVFGETD ACELWMGEKE KWLAQMEIPD TLEDLEVVQH RFDILDQEMK
TLMTQIDGVN LAANSLVESG HPRSGEVKQY QDHLNTRWQA FQTMVSDRRE AVGSALRVHN
YCVDCEETSK WILDKTKVVE STKDLGRDLT GVIAIQRKLS GLERDVAAIQ TRVGALERES
RWLMESHPEL KEDIGRRQAY VEELWQGLQQ ALQGQEASLG EASQLQAFLQ ELDDFQGWLS
MAQKAVASED TPESLPEAEQ LLQQHAAIKD EIDGHQDSYE HVKASGEKVL RGQTDPEYLL
LGQRLEGLGT GWDALRRMWE SRGHFLAQCL GFQEFQKDAK QAEAILSNQE YTLAHLETPD
SLEAAEAGIR KFEDFLVSME NNQDKVLSPV DSGNKLVAEG NLYADKIKEK VQSIEDRHRK
NNEKAQEASV LLKDNLELQN FLQNCQELTL WINDKLLTSQ DVSYDEARNL HNKWLKHQAF
MAELASHEGW LESIDAEGKQ LMEEKPQFAA LVSQRLEALH RLWDELQATT KEKAQQLSAA
RSSDLRSKTH ADLNKWISAM EDQLRSDDPG KDLTSVNRML AKLKARRVED QVNVRKEELG
ELFAQMPSLD EEEGGADMSI EKRFLDLLEP LGKRKKQLES SRAKLQISRD LEDETLWVEE
RLPLAQSSDY GINLQTVQLF MKKNQTLQNE ILGHAPRVED VLQRGQRLVE EAEIDCGDIE
ERLGHLQSSW DTLREAAAGR LRRLRDASEA QQYYLDAGEA EAWISEQELY VISDETPKDE
EGAIVMLKRH LRQQRAVEEY GRNIKQLAGR AQGLLAAGHP EGEQIIRLQG QVDKQYAGLK
DMAEERKRKL ENMYHLFQLK READDLEQWI AEKELVASSP EMGQDFDHVT LLRDKFRDFA
RETGAIGQER VDNVNAIIER LIDAGHGEAA TIAEWKDGLN EMWADLLELI DTRMQLLAAS
YDLHRYFYTG TEILGLIDEK HRELPEDVGL DASTAESFHR VHTAFERELH LLGVQVQQFQ
DVATRLQMAY AGEKADAIQD KEREVSAAWQ ALLDACAGRR TQLVDTADKF RFFSMARDLL
SWMESIIRQI ETQERPRDVS SVELLMKYHQ GIRAEIDTRS KNFNACLELG ESLLQREHQA
SEEIREKLQQ VMSRRKEMNE KWEARWERLS MLLEVCQFSR DASVAEAWLI AQEPYLASRD
FGHTVDSVEK LIKRHEAFEK STASWAERFA ALEKPTTLEL KERQIPETPV EETGPQEEEG
ETAGEGPRGP HRAATERTSP GEEERQWPQD LQPPPPPGPQ KEGQEEKSGG DERPATEPPK
ILDTPLSEGD EPITLPAQQD HGHSVQMEGY LGRKHDLEGP NKKASNRSWN HLYCVLRNSE
LTFYKDAKNL ALGVPYHGEE PLALRHAICE IAANYKKKKH VFKVRLSNGS EWLFHGKDEE
EMLSWLQGVS TAINESQSIR VKAQSLPLPS ITGPDTSLGK KDKEKRFSFF PKKK
//
