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Database: UniProt
Entry: G1P234_MYOLU
LinkDB: G1P234_MYOLU
Original site: G1P234_MYOLU 
ID   G1P234_MYOLU            Unreviewed;      2369 AA.
AC   G1P234;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=SPTB {ECO:0000313|Ensembl:ENSMLUP00000003910.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000003910.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000003910.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000003910.2}
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   EMBL; AAPE02022573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02022574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000003910; -.
DR   Ensembl; ENSMLUT00000004293.2; ENSMLUP00000003910.2; ENSMLUG00000004280.2.
DR   eggNOG; KOG0517; Eukaryota.
DR   GeneTree; ENSGT00940000158908; -.
DR   HOGENOM; CLU_000146_1_2_1; -.
DR   InParanoid; G1P234; -.
DR   OMA; EPADMTS; -.
DR   TreeFam; TF313446; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0014731; C:spectrin-associated cytoskeleton; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
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:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
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; 8.
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:UP000001074};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          57..161
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          2219..2329
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2081..2113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2155..2218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          461..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2179..2193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2369 AA;  272158 MW;  E82BEF6A27ECA6D2 CRC64;
     PADMTSATEF ENVANQPPYS RINARWDAPD DELDNDNSSA RLFERSRIKA LADEREVVQK
     KTFTKWVNSH LARKSCRITD LYKDLRDGQM LIKLLEVLSG EMLPKPTKGK MRIHCLENVD
     KALQFLKEQR VHLENMGSHD IVDGNHRLVL GLIWTIILRF QIQDIVVPEG PEGRETRSAK
     DALLLWCQMK TAGYPHVNVT NFTSSWKDGL AFNALIHKHR PDLIDFDKLK DSNARHNLEH
     AFDVAERQLG IIPLLDPEDV FTENPDEKSI ITYVVAFYHY FSKMKVLAVE GKRIGKVIDH
     AIETEKMIEK YSGLASDLLT WIEQTITVLN SRKFANSLTG VQQQLQAFST YRTVEKPPKF
     QEKGNLEVLL FTIQSRMRAN NQKVYTPHDG KLVSDINRAW ESLEEAEYRR ELALRNELIR
     QEKLEQLARR FDRKAAMRET WLNENQRLVA QDNFGYDLAA VEAAKKKHEA IETDTAAYEE
     RVRALEDLAQ ELEKENYHDQ KRITARKDNI LRLWSYLQEL LASRRQRLET TLALQKLFQD
     MLHSIDWMDE IKAHLLSAEF GKHLLEVEDL LQKHKLMEAD IAIQGDKVKA INTATLQFTE
     GKGYQPCDPQ VIQDRVSHLE QCFEELSNMA AGRKAQLEQS KRLWKFFWEM DEAESWIKEK
     EQIYSSLDYG KDLTSVLILQ RKHKAFEDEL RGLDTHLDQI FQEAEGMVAR KQFGHPQIEA
     RIKEVSAQWD QLKELAAFRK KNLQDAENFF QFQGDADDLK AWLQDAHKLL SGEDVGQDEG
     ATRALGKKHK DFLEELEESR AVMEHLERQA QGFPQEFRDS PDVTNRLQAL RDLYQQVVAQ
     ADLRRQKLQE ALDLYTVFGE TDACELWMGE KEKWLAQMEI PDTLEDLEVV QHRFDILDQE
     MKTLMTQIDG VNLAANSLVE SGHPRSGEVK QYQDHLNTRW QAFQTMVSDR REAVGSALRV
     HNYCVDCEET SKWILDKTKV VESTKDLGRD LTGVIAIQRK LSGLERDVAA IQTRVGALER
     ESRWLMESHP ELKEDIGRRQ AYVEELWQGL QQALQGQEAS LGEASQLQAF LQDLDDFQGW
     LSMAQKAVAS EDTPESLPEA EQLLQQHAAI KDEIDGHQDS FERVKASGEK VLQGQMDPEY
     LLLGQRLEGL GTGWDALRRM WESRGHFLAQ CLGFQEFQKD AKQAEAILSN QEYTLAHLET
     PDSLEAAEAG IRKFEDFLVS MENNQDKVLN PVDSGNKLVA EGNLYADKIK EKVQSIEDRH
     RKNNEKAQEA SVLLKDNLEL QNFLQNCQEL TLWINDKLLT SQDVSYDEAR NLHNKWLKHQ
     AFMAELASHE GWLESIDAEG KQLMEEKPQF AALVSQRLEA LHRLWDELQA TTKEKAQQLS
     AARSSDLRSK THADLNKWIS AMEDQLRSDD PGKDLTSVNR MLAKLKRVED QVNVRKEELG
     ELFAQMPSLD EEEGGADMSI EKRFLDLLEP LGKRKKQLES SRAKLQISRD LEDETLWVEE
     RLPLAQSSDY GINLQTVQLF MKKNQTLQNE ILGHAPRVED VLQRGQRLVE EAEIDCGDIE
     ERLGHLQSSW DTLREAAAGR LQRLRDASEA 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 GIRAEIETRS KNFNACLELG ESLLQREHQA
     SEEIREKLQQ VMSRRKEMNE KWEARWERLS MLLEVCQFSR DASVAEAWLI AQEPYLASRD
     FGHTVDSVEK LIKRHEAFEK STASWAERFA ALEKPTTLEL KERQIPEPPV EETGQKQPPA
     SIPHCSLSSG QFPKGRRMEV KVWEENVGSQ ASILLSSRPR AEPQQGVLPL CAPEQGEEER
     QWPQDLQPPP PPGPQKEGQE EKSGGDERPA TEPLKVLDTP LSEGDEPITL PAQQDHGHSV
     QMEGYLGRKH DLEGPNKKAS NRSWNHLYCV LRNSELTFYK DAKNLALGVP YHGEEPLALR
     HAICEIAANY KKKKHVFKLR LSNGSEWLFH GKDEEEMLSW LQGVSTAINE SQSIRVKAQS
     LPLPSITGPD TSLGKKDKEK RFSFFPKKK
//
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