SPTB1_MOUSE
ID SPTB1_MOUSE Reviewed; 2128 AA.
AC P15508;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Spectrin beta chain, erythrocytic;
DE AltName: Full=Beta-I spectrin;
GN Name=Sptb; Synonyms=Spnb-1, Spnb1, Sptb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8219239;
RA Bloom M.L., Birkenmeier C.S., Barker J.E.;
RT "Complete nucleotide sequence of the murine erythroid beta-spectrin cDNA
RT and tissue-specific expression in normal and jaundiced mice.";
RL Blood 82:2906-2914(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1055-1290.
RX PubMed=3307952;
RA Cioe L., Laurila P., Meo P., Krebs K., Goodman S., Curtis P.J.;
RT "Cloning and nucleotide sequence of a mouse erythrocyte beta-spectrin
RT cDNA.";
RL Blood 70:915-920(1987).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-1289 AND THR-2072,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal network
CC underlying the erythrocyte plasma membrane. It associates with band 4.1
CC and actin to form the cytoskeletal superstructure of the erythrocyte
CC plasma membrane.
CC -!- SUBUNIT: Composed of nonhomologous chains, alpha and beta, which
CC aggregate to form dimers, tetramers, and higher polymers.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of the
CC plasma membrane via another protein, ankyrin, which binds to beta-
CC spectrin and mediates the binding of the whole complex to a
CC transmembrane protein band 3. The interaction of erythrocyte spectrin
CC with other proteins through specific binding domains lead to the
CC formation of an extensive subplasmalemmal meshwork which is thought to
CC be responsible for the maintenance of the biconcave shape of human
CC erythrocytes, for the regulation of plasma membrane components and for
CC the maintenance of the lipid asymmetry of the plasma membrane.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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DR EMBL; S66283; AAB28600.1; -; mRNA.
DR EMBL; M18641; AAA40126.1; -; mRNA.
DR PIR; A45929; A45929.
DR AlphaFoldDB; P15508; -.
DR SMR; P15508; -.
DR IntAct; P15508; 3.
DR MINT; P15508; -.
DR STRING; 10090.ENSMUSP00000021458; -.
DR iPTMnet; P15508; -.
DR PhosphoSitePlus; P15508; -.
DR jPOST; P15508; -.
DR MaxQB; P15508; -.
DR PaxDb; P15508; -.
DR PeptideAtlas; P15508; -.
DR PRIDE; P15508; -.
DR ProteomicsDB; 261641; -.
DR ABCD; P15508; 1 sequenced antibody.
DR MGI; MGI:98387; Sptb.
DR eggNOG; KOG0517; Eukaryota.
DR InParanoid; P15508; -.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR ChiTaRS; Sptb; mouse.
DR PRO; PR:P15508; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P15508; protein.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IMP:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
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; SSF47576; 1.
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; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2128
FT /note="Spectrin beta chain, erythrocytic"
FT /id="PRO_0000073460"
FT DOMAIN 54..158
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 173..278
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 303..411
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 416..517
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 521..627
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 630..733
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 736..838
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 845..942
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 950..1050
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1054..1157
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1162..1250
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1267..1368
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1381..1455
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1473..1574
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1576..1680
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1682..1784
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1789..1890
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1897..1997
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2004..2064
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..275
FT /note="Actin-binding"
FT REGION 2062..2108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2062..2082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2064
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2072
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
FT MOD_RES 2119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11277"
SQ SEQUENCE 2128 AA; 245250 MW; 10E576111106DFE1 CRC64;
MTSATEFENV GNQPPFSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF
TKWVNSHLAR VSCRISDLYK DLRDGRMLIK LLEVLSGEML PRPTKGKMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR EQRSAKDALL
LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV
AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
EKMIEKYSGL ASDLLTWIEQ TISVLNSRKF ANSLSGVQQQ LQAFSTYRTV EKPPKFQEKG
NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYQRELAL RSELIRQEFD
RKAAMRETWL NENQRLVTQD NFGYDLAAVE AAKKKHEAIE TDTAAYEERV KALEDLAQEL
EKENYHDQKR IIARKDNILR LWSYLQELLR SRRQRLEATL ALQKLFQDML HSIDWMDEIK
AHILSAEFGK HLLEVEDLLQ KHKLMEADIA IQGDKVKAIT AATLQFAEGK GYQPCDPQVI
QDRVSHLEQC FSELSNMAAG RKAQLEQSKR LWKFFWEMDE AESWIKEKEQ IYSSLDYGKD
LTSVLILQRK HKAFEDELRG LDAHLKQIFQ EADDMVAQKQ FGHPQIETRV KEVSAQWDHL
KELAAFRKKD LQDAENFFQF QGDADDLKAW LQDAHRLLSG EDVGQDEGAT RALGKKHKEF
LEELEESRGV MEHLEHQAQG FPEEFRDSPD VTNRLQALRK LYQQVLTQAE LRGHKLQEAL
DLYTVFGESD ACELWMTEKG KWLDQMDIPN TLEDLEVVQH RFDILDQEMK TLMAQIDGVN
LAANNLVESG HPRSGEVKQY QDRLNKRWQA FQAVVSEQRE AVDSALRVNN YCVDCEETSK
WIMDKTKVVE STKDLGQDLA GVIAIQRKLS GLERDVLAIR DRVSALERES QYLMESHPEQ
KEDIGQRQAD VEKLWKGLQD ALQGQELSLG EASKLQAFLQ DLDDFKAWLS MAQKAVASED
MPESLPEAEQ LLQQHAAIKE EIDAHRDDYH RVKASGEKVI EGQTDPDYQL LGQRLEGLDT
DWDALRRMWE SRGNTLTQCL GFQEFQKDAK QAEAILSNQE YTLAHLEPPD SLAAAEAGIR
KFEDFLVSME NNRDKILSPV DSGNKLVAEG NLYSNKIMEK VQLIEDRHKK NNEKAQEATV
LLKDNLELQN FLQNCKELTL WINDKLLTSP DVSYDEARNL HNKWMKHQAF MAELASHQGW
LENIDAEGRQ LMAEKPQFKD VVSERLEALH KLWEELQSTA KAKAEQLSAA RSSDLRLQTH
ADLNKWIGAM EDQLRSDDLG KDLTTVNRML AKLKRVEEQV NLRKEELEEL FADAPSLGAE
AGDTDMSIEK RFLDLLEPLG RRKKQLELSK AKLQISRDLE DETLWVEERL PLAQSADYGT
NLQTVQLFMK KNQTLQNEIL GHAPRVEDVL RRGQELVKAA EIDCQDIEER LGHLQSSWDT
LREAAAGRLQ RLRDAHEAQQ YYLDAGEAEA WISEQELYVF SDEPPKDEEG AIVMLKRHLR
QQRTVEEYGR NIKQLAGRAQ SLLSAGHPEG EQIIRLQGQV DKQYAGLKDM AEERRRRLEN
MYHLFQLKRE ADDLEQWITE KEMVASSQEM GQDFDHVTML RDKFRDFARE TGAIGQERVD
NVTIIERLID AGHSEAATIA EWKDGLNDMW ADLLELIDTR MQLLAASYDL HRYFYTGTEI
LGLIDEKHRE LPEDVGLDAS TAESFHRVHT AFERELHLLG VQVQQFQDVA TRLQTAYAGE
KADAIQSKEQ EVSAAWQALL DACAGRRAQL VDTADKFRFF SMVRDLLSWM ESIIRQIETQ
ERPRDVSSVE LLLKYHQGIK AEINTRAKNF STCLELGESL LQRQHQASDE IREKLQQVIS
RRQEMNDKWE ARSDRLHMLL EVCQFSRDAS VAEAWLIAQE PYLASRDFGH TVDSVEKLIK
RHEAFEKSTA SWAERFAALE KPTTLELKER QTPERPTEEP GPQEEEGETA GEAPQVHHAA
TERTSPVSFM SRLSSSWESL LPEPAHPF
