(data stored in ACNUC32233 zone)

HOGENOM: MOUSE11_PE522

ID   MOUSE11_PE522                        STANDARD;      PRT;   2363 AA.
AC   MOUSE11_PE522; Q62261; A2AFU1; Q3TEM7; Q5SQL8; Q5SQL9; Q9QWJ7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Spectrin beta chain, brain 1;AltName: Full=Beta-II
DE   spectrin;AltName: Full=Embryonic liver fodrin;AltName: Full=Fodrin beta
DE   chain;AltName: Full=Spectrin, non-erythroid beta chain 1;
DE   (MOUSE11.PE522).
GN   Name=Sptbn1; Synonyms=Elf, Spnb-2, Spnb2, Sptb2;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE11.PE522.
CC       Mus musculus chromosome 11 NCBIM37  sequence 1..121843856 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:SPTB2_MOUSE
CC   -!- FUNCTION: Fodrin, which seems to be involved in secretion,
CC       interacts with calmodulin in a calcium-dependent manner and is
CC       thus candidate for the calcium-dependent movement of the
CC       cytoskeleton at the membrane.
CC   -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC       capable to form dimers which can further associate to tetramers.
CC       Interacts with ANK2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       myofibril, sarcomere, M line. Note=Colocalizes with ANK2 in a
CC       distinct intracellular compartment of neonatal cardiomyocytes.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62261-1; Sequence=Displayed;
CC       Name=2; Synonyms=Elf3;
CC         IsoId=Q62261-2; Sequence=VSP_026057, VSP_026058, VSP_026059;
CC         Note=Phosphorylated on Ser-14 (By similarity), Ser-8 and Ser-10;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, heart, kidney
CC       and liver (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in brain, heart and
CC       liver throughout embryonic development. Isoform 1 is mainly
CC       expressed in neonatal developing ventricular cardiomyocytes.
CC   -!- PTM: Isoform 2 is phosphorylated on Ser-8 and Ser-10.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 17 spectrin repeats.
CC   -!- GENE_FAMILY: HOG000007281 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000020315;ENSMUST00000006629;ENSMUSP00000006629.
DR   EMBL; AF017112; - ;
DR   EMBL; AF047686; - ;
DR   EMBL; AK051630; - ;
DR   EMBL; AK169544; - ;
DR   EMBL; AK220456; - ;
DR   EMBL; AL672225; - ;
DR   EMBL; AL731792; - ;
DR   EMBL; BC024833; - ;
DR   EMBL; M74773; - ;
DR   EMBL; U73171; - ;
DR   UniProtKB/Swiss-Prot; Q62261; A2AFU1; Q3TEM7; Q5SQL8; Q5SQL9; Q9QWJ7; -.
DR   EMBL; M74773; AAC42040.1; -; mRNA.
DR   EMBL; AF017112; AAD01616.1; -; mRNA.
DR   EMBL; AL731792; CAI24366.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAI24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL731792; CAI24367.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAI24367.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAI25429.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAI25429.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAI25430.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAI25430.1; JOINED; Genomic_DNA.
DR   EMBL; AL731792; CAM16973.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAM16973.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAM22716.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAM22716.1; JOINED; Genomic_DNA.
DR   EMBL; AK169544; BAE41221.1; -; mRNA.
DR   IPI; IPI00121892; -.
DR   IPI; IPI00319830; -.
DR   RefSeq; NP_033286.2; NM_009260.2.
DR   RefSeq; NP_787030.2; NM_175836.2.
DR   UniGene; Mm.123110; -.
DR   UniGene; Mm.466085; -.
DR   PDB; 1BTN; X-ray; 2.00 A; A=2199-2304.
DR   PDB; 1MPH; NMR; -; A=2199-2304.
DR   PDBsum; 1BTN; -.
DR   PDBsum; 1MPH; -.
DR   ProteinModelPortal; Q62261; -.
DR   SMR; Q62261; 49-283, 297-2086, 2197-2332.
DR   IntAct; Q62261; 7.
DR   STRING; Q62261; -.
DR   PhosphoSite; Q62261; -.
DR   PRIDE; Q62261; -.
DR   Ensembl; ENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315.
DR   Ensembl; ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315.
DR   Ensembl; ENSMUST00000102838; ENSMUSP00000099902; ENSMUSG00000020315.
DR   GeneID; 20742; -.
DR   KEGG; mmu:20742; -.
DR   UCSC; uc007ihs.1; mouse.
DR   UCSC; uc007iht.1; mouse.
DR   CTD; 20742; -.
DR   MGI; MGI:98388; Spnb2.
DR   eggNOG; roNOG06871; -.
DR   InParanoid; Q62261; -.
DR   OMA; KEGEDMI; -.
DR   OrthoDB; EOG4WWRHM; -.
DR   NextBio; 299385; -.
DR   ArrayExpress; Q62261; -.
DR   Bgee; Q62261; -.
DR   CleanEx; MM_SPNB2; -.
DR   Genevestigator; Q62261; -.
DR   GermOnline; ENSMUSG00000020315; Mus musculus.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
DR   GO; GO:0007184; P:SMAD protein import into nucleus; IDA:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 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; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   HOGENOMDNA; MOUSE11.PE522; -.
KW   ENSMUSG000000203155old_1320000031; ENSMUSP000000066291old_1320000031;
KW   P70435_MOUSE; Q5DTR4_MOUSE; Q8BQ35_MOUSE; Q8R1C2_MOUSE; Q9R1Y9_MOUSE;
KW   AF047686; AK051630; AK169544; AK220456; AL672225; AL731792; BC024833;
KW   U73171;
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative splicing; Calmodulin-binding; Cell membrane;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat.
SQ   SEQUENCE   2363 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
     TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
     LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
     AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
     EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
     NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
     EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
     VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
     MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG
     YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
     LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII
     YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ
     SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL
     RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
     QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
     HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
     KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR
     TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
     RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
     LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
     REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
     AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
     KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ
     SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW
     VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA
     EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK
     AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY
     AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF
     REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
     LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV
     RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV
     RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR
     KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL
     SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
     PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS
     KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS
     WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD
     GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS
     PGKREKDKEK DKEKRFSLFG KKK
//

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