ID A0A287BDN2_PIG Unreviewed; 2365 AA.
AC A0A287BDN2; A0A286ZK87;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSSSCP00000054202.2,
GN ECO:0000313|VGNC:VGNC:93436};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000054202.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000054202.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000054202.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000054202.2}
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 STRING; 9823.ENSSSCP00000031872; -.
DR PaxDb; 9823-ENSSSCP00000019960; -.
DR Ensembl; ENSSSCT00000062533.3; ENSSSCP00000031872.2; ENSSSCG00000040786.3.
DR Ensembl; ENSSSCT00000065413.3; ENSSSCP00000054202.2; ENSSSCG00000040786.3.
DR VGNC; VGNC:93436; SPTBN1.
DR GeneTree; ENSGT00940000154864; -.
DR Reactome; R-SSC-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-SSC-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SSC-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SSC-9013420; RHOU GTPase cycle.
DR Reactome; R-SSC-9013424; RHOV GTPase cycle.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000040786; Expressed in ovary and 40 other cell types or tissues.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031430; C:M band; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase 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:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0021556; P:central nervous system formation; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0071709; P:membrane assembly; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IEA:Ensembl.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd21316; CH_SPTBN1_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:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 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; 15.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR002297};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287BDN2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 54..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 173..278
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2198..2308
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2090..2197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2310..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 991..1032
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1097..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1423..1457
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1854..1881
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2090..2106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2107..2197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2310..2341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2365 AA; 274550 MW; 07F41A7512393E79 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 ALVEADIGIQ AERVRGVNAS AQKFATDGEG
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERIA
YIREQWAHLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ
SLVKKHKDVA EEIANYRPTI DSLHEQAGAL PQEHAESPDV RGRLAGIEER YKEVAELTRL
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LRNREASLGE ASKLQQFLRD LDDFQSWLSR
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
RQRLQALDTG WNELHKMWEN RQNLLSQSHA HQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQAMLENQM EVRKKEIEEL
QSQAQALSQE GKSTDEVDSK RLTVQTKFME LLEPLNERKQ NLLASKEIHQ FNRDVEDEIL
WVGERMPLAT STDHGHNLQT VQLLIKKNQT LQKEIQGHQP RIDDIFERSQ NIVADSSSLS
AEAIRQRLAD LKQLWGQLIE ETEKRHRRLE EAHRAQQYYF DAAEAEAWMS EQELYMMSEE
KAKDEQSAVS MLKKHQILEQ AVEDYAETVH QLSKTSRALV ADSHPESERI SMRQSKVDKL
YAGLKDLAEE RRGKLDERHR LFQLNREVDD LEQWIAEREV VAGSHELGQD YEHVTMLQER
FREFARDTGN IGQERVDTVN HMADELINSG HSDAATIAEW KDGLNEAWAD LLELIDTRTQ
ILAASYELHK FYHDAKEIFG RIQDKHKKLP EELGRDQNTV ETLQRMHTTF EHDIQALGTQ
VRQLQEDAAR LQAAYAGDKA DDIQKRENEV LEAWKALLDA CEGRRVRLVD TGDKFRFFSM
VRDLMLWMED VIRQIEAQEK PRDVSSVELL MNNHQGIKAE IDARNDSFTT CIELGKSLLA
RKHYASEEIK EKLLQLTDKR KEMIDKWEDR WEWLRLILEV HQFSRDASVA EAWLLGQEPY
LSSREIGQSV DEVEKLIKRH EAFEKSAATW DERFSALERL TTLELLEVRR QQEEEERKRR
PPSPEPSTKV SEETESQQQW DTSKGEQVSQ NGLPTEQGSP RMAETVDTSE MVNGAAEQRT
SSKESSPIPS PTSDRKAKTS LPAQSAATLP ARTQETPSAQ MEGFLNRKHE WEAHNKKASS
RSWHNVYCVI NNQEMGFYKD AKTAASGIPY HSEVPVSLKE AICEVALDYK KKKHVFKLRL
NDGNEYLFQA KDDEEMNTWI QAISSAISSD KHEVSASTQS TPASSRAQTL PTSAVTITSE
SSPGKREKDK EKDKEKRFSL FGKKK
//
