ID A0A0G2JZY6_RAT Unreviewed; 2152 AA.
AC A0A0G2JZY6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=Sptbn1 {ECO:0000313|Ensembl:ENSRNOP00000071233.2,
GN ECO:0000313|RGD:727922};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000071233.2, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000071233.2, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071233.2,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000071233.2}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071233.2};
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 jPOST; A0A0G2JZY6; -.
DR Ensembl; ENSRNOT00000084595.2; ENSRNOP00000071233.2; ENSRNOG00000005434.8.
DR AGR; RGD:727922; -.
DR RGD; 727922; Sptbn1.
DR VEuPathDB; HostDB:ENSRNOG00000005434; -.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000005434; Expressed in lung and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0G2JZY6; baseline and differential.
DR GO; GO:0030673; C:axolemma; ISO:RGD.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:RGD.
DR GO; GO:0032437; C:cuticular plate; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031430; C:M band; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0021556; P:central nervous system formation; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR GO; GO:0071709; P:membrane assembly; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0007009; P:plasma membrane organization; ISO:RGD.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISO:RGD.
DR CDD; cd21246; CH_SPTB-like_rpt1; 1.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd00176; SPEC; 7.
DR Gene3D; 1.20.58.60; -; 12.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_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; 14.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JZY6};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 41..145
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 160..265
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 2074..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 976..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1082..1109
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1407..1441
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1838..1865
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2074..2090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2094..2152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2152 AA; 250778 MW; A34EEEE0DD60B602 CRC64;
MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW VNSHLARVSC
RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM
GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV
NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP
EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD
LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM
RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM
RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELEAESY
HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLLLS
QDYGKHLLGV EDLLQKHALV EADIAIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV
AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS DDYGKDLTSV
MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE IRERISYIRE QWANEQLSAI
RKKRLEEASL LHQFQADADD IDAWMLDILK IVSSNDVGHD EYSTQSLVKK HKDVAEEISN
YRPTIDTLHE QAGALPQAHA ESPDVKGRLA GIEERYKEVA ELTRLRKQAL QDTLALYKMF
SEADACELWI DEKEQWLNNM QIPEKLEDLE VIQHRFESLE PEMNNQASRV AVVNQIARQL
MHSGHPSEKE IRAQQDKLNT RWSQFRELVD RKKDALLSAL SIQNYHLECN ETKSWIREKT
KVIESTQDLG NDLAGVMALQ RKLTGMERDL VAIEAKLSDL QKEAEKLESE HPDQAQAILS
RLAEISDVWE EMKTTLKNRE ASLGEASKLQ QFLRDLDDFQ SWLSRTQTAI ASEDMPNTLT
EAEKLLTQHE NIKNEIDNYE EDYQKMRDMG EMVTQGQTDA QYMFLRQRLQ ALDTGWNELH
KMWENRQNLL SQSHAYQQFL RDTKQAEAFL NNQEYVLAHT EMPTTLEGAE AAIKKQEDFM
TTMDANEEKI NAVVETGRRL VSDGNINSDR IQEKVDSIDD RHRKNREAAS ELLMRLKDNR
DLQKFLQDCQ ELSLWINEKM LTAQDMSYDE ARNLHSKWLK HQAFMAELAS NKEWLDKIEK
EGMQLISEKP ETEAVVKEKL TGLHKMWEVL ESTTQTKAQR LFDANKAELF TQSCADLDKW
LHGLESQIQS DDYGKDLTSV NILLKKQQML ENQMEVRKKE IEELQSQAQA LSQEGKSTDE
VDSKRLTVQT KFMELLEPLN ERKHNLLASK EIHQFNRDVE DEILWVGERM PLATSTDHGH
NLQTVQLLIK KNQTLQKEIQ GHQPRIDDIF ERSQNIITDS SSLNAEAIRQ RLADLKQLWG
LLIEETEKRH RRLEEAHKAQ QYYFDAAEAE AWMSEQELYM MSEEKAKDEQ SAVSMLKKHQ
ILEQAVEDYA ETVHQLSKTS RALVADSHPE SERISMRQSK VDKLYAGLKD LAEERRGKLD
ERHRLFQLNR EVDDLEQWIA EREVVAGSHE LGQDYEHVTM LQERFREFAR DTGNIGQERV
DTVNHMADDL INSGHSDAAT IAEWKDGLNE AWADLLELID TRTQILAASY ELHKFYHDAK
EIFGRIQDKH KKLPEELGRD QNTVETLQRM HTTFEHDIQA LGTQVRQLQE DAARLQAAYA
GDKADDIQKR ENEVLEAWKS LLDACEGRRV RLVDTGDKFR FFSMVRDLML WMEDVIRQIE
AQEKPRDVSS VELLMNNHQG IKAEIDARND SFTACIELGK ALLARKHYAS EEIKEKLLQL
TEKRKEMIDK WEDRWEWLRL ILEVHQFSRD ASVAEAWLLG QEPYLSSREI GQSVDEVEKL
IKRHEAFEKS AATWDERFSA LERLTTLELL EVRRQQEEEE RKRRPPSPEP SAKVSEEAES
QQWDTSKGDQ VSQNGLPAEQ GSPRVSYRSQ TYQNYKNFNS RRTASDHSWS GL
//
