ID A0A2R8ZQ01_PANPA Unreviewed; 2364 AA. AC A0A2R8ZQ01; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 24-JAN-2024, entry version 24. DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297}; GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSPPAP00000004886.1}; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000004886.1, ECO:0000313|Proteomes:UP000240080}; RN [1] {ECO:0000313|Ensembl:ENSPPAP00000004886.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the spectrin family. CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJFE02108940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJFE02108941; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003830884.1; XM_003830836.2. DR SMR; A0A2R8ZQ01; -. DR Ensembl; ENSPPAT00000022371.1; ENSPPAP00000004886.1; ENSPPAG00000020369.1. DR GeneTree; ENSGT00940000154864; -. DR OrthoDB; 2872403at2759; -. DR Proteomes; UP000240080; Unplaced. DR Bgee; ENSPPAG00000020369; Expressed in heart and 6 other cell types or tissues. DR GO; GO:0016020; C:membrane; IEA:UniProt. DR GO; GO:0008091; C:spectrin; IEA:InterPro. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. 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 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; 14. 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|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR002297}; KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR002297}; KW Reference proteome {ECO:0000313|Proteomes:UP000240080}; 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 2197..2307 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT REGION 2089..2196 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2309..2364 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 1422..1456 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1853..1880 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 2089..2105 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2108..2178 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2309..2340 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2341..2357 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2364 AA; 274609 MW; 1770C3B0EB07B892 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 VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ 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 RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM VNGATEQRTS SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM EGFLNRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDA KTAASGIPYH SEVPVSLKEA VCEVALDYKK KKHVFKLRLN DGNEYLFQAK DDEEMNTWIQ AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES SPGKREKDKE KDKEKRFSLF GKKK //