ID A0A2K5P4M4_CERAT Unreviewed; 2311 AA.
AC A0A2K5P4M4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSCATP00000044645.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000044645.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000044645.1}
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}.
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DR Ensembl; ENSCATT00000069087.1; ENSCATP00000044645.1; ENSCATG00000044787.1.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000044787; Expressed in frontal cortex and 12 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; -; 11.
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; 16.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 2.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00033; CH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00150; SPEC; 16.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 12.
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|PIRNR:PIRNR002297};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
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 2144..2254
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2036..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2256..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..438
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 938..979
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1044..1071
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1369..1403
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1800..1827
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2036..2052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2288..2304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2311 AA; 268098 MW; 572BD8C98726673B 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 DINKDNFGFD LPAVEAATKK HEAIETDIAA
YEERVQAVVA VARELEAENY HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI
FQEMLYIMDW MDEMKVLVLS QDYGKHLLGV EDLLQKHTLV EADIGIQAER VRGVNASAQK
FATDGEGYKP CDPQVIRDRV AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW
IREKEKILSS DDYGKDLTSV MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE
KIRERIIYIR EQWANLEQLS AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LKIVSSSDVG
HDEYSTQSLV KKHKDVAEEI ANYRPTLDTL HEQASALPQE HAESPDVRGR LSGIEERYKE
VAELTRLRKQ ALQDTLALYK MFSEADACEL WIDEKEQWLN NMQIPEKLED LEVIQHRFES
LEPEMNNQAS RVAVVNQIAR QLMHSGNPSE KEIKAQQDKL NTRWSQFREL VDRKKDALLS
ALSIQNYHLE CNETKSWIRE KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS
DLQKEAEKLE SEHPDQAQAI LSRLAEISDV WEEMKTTLKN REASLGEASK LQQFLRDLDD
FQSWLSRTQT AIASEDMPNT LTEAEKLLTQ HENIKNEIDN YEEDYQKMRD MGEMVTQGQT
DAQYMFLRQR LQALDTGWNE LHKMWENRQN LLSQSHAYQQ FLRDTKQAEA FLNNQEYVLA
HTEMPTTLEG AEAAIKKQED FMTTMDANEE KINAVVETGR RLVSDGNINS DRIQEKVDSI
DDRHRKNRET ASELLMRLKD NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW
LKHQAFMAEL ASNKEWLDKI EKEGMQLISE KPETEPVVKE KLTGLHEMWE VLESTTQTKA
QRLFDANKAE LFTQSCADLD KWLHGLESQI QSDDYGKDLT SVNILLKKQQ MLENQMEVRK
KEIEELQSQA QALSQEGKST DEVDSKRLTV QTKFMELLEP LNERKHNLLA SKEIHQFNRD
VEDEILWVGE RMPLATSTDH GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIVT
DSSSLNAEAI RQRLADLKQL WGLLIEETEK RHRRLEEAHR AQQYYFDAAE AEAWMSEQEL
YMMSEEKAKD EQSAVSMLKK HQILEQAVED YAETVHQLSK TSRALVADSH PESERISMRQ
SKVDKLYAGL KDLAEERRGK LDERHRLFQL NREVDDLEQW IAEREVVAGS HELGQDYEHV
TMLQERFREF ARDTGNIGQE RVDTVNHMAD ELINSGHSDA ATIAEWKDGL NEAWADLLEL
IDTRTQILAA SYELHKFYHD AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI
QALGTQVRQL QEDAARLQAA YAGDKADDIQ KRENEVLEAW KSLLDACESR RVRLVDTGDK
FRFFSMVRDL MLWMEDVIRQ IEAQEKPRDV SSVELLMNNH QGIKAEIDAR NDSFTTCIEL
GKSLLARKHY ASEEIKEKLL QLTEKRKEMI DKWEDRWEWL RLILEVHQFS RDASVAEAWL
LGQEPYLSSR EIGQSVDEVE KLIKRHEAFE KSAATWDERF SALERLTTLE LLEVRRQQEE
EERKRRPPSP EPSTKVSEEA ESQQQWDTAK GEQVSQNGLP AEQGSPRMAE TVDTSEMVNG
ATEQRTSSKE SSPIPSPTSD RKAKTALPAQ SAATLPARTQ ETPSAQMEGF LNRKHEWEAH
NKKASSRSWH NVYCVINNQE MGFYKDAKTA ASGIPYHSEV PVSLKEAVCE VALDYKKKKH
VFKLRLNDGN EYLFQAKDDE EMNTWIQAIS SAISSDKHEV SASTQSTPAS SRAQTLPTSV
VTITSESSPG KREKDKEKDK EKRFSLFGKK K
//
