ID S4RS86_PETMA Unreviewed; 2362 AA.
AC S4RS86;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000008075.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000008075.1}
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; 7757.ENSPMAP00000008075; -.
DR Ensembl; ENSPMAT00000008111.1; ENSPMAP00000008075.1; ENSPMAG00000007298.1.
DR GeneTree; ENSGT00940000154864; -.
DR HOGENOM; CLU_000146_1_2_1; -.
DR OMA; EGEGMIA; -.
DR Proteomes; UP000245300; Unplaced.
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; cd21317; CH_SPTBN2_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:SF447; SPECTRIN BETA CHAIN; 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; 13.
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:UP000245300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 57..161
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 176..281
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2200..2312
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2092..2196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2309..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..494
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 994..1028
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1100..1127
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2092..2123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2124..2154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2174..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2309..2339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2362 AA; 273472 MW; 0CBD0D6DCD9F8113 CRC64;
AMTAVSKDLE GSMDIQQQYE SINNRWEASE EDWDNENSSA RLFERSRIKA LADEREAVQK
KTFTKWVNSH LARVSCRITD LYTDLRDGRM LIKLLEVLSG EKLPKPTRGK MRIHCLENVD
KALQFLKEQK VHLENMGSHD IVDGNHRLIL GLIWTIILRF QIQDISVETE DNKERRSAKD
ALLLWCQMKT AGYQNVNIHN FTTSWRDGLA FNAIVHKHRP DLIEFDKLKK SNAHHNLQNA
FNIAEQKLGL TKLLDPEDIS VDQPDEKSII TYVVTYYHYF SKMKALAVEG KRIGKVLESA
IETDQMIDKY ETLASELLEW IEQTIIILNN RKFANSLTGV QQQLQAFSTY RTVEKPNKFT
EKGNLEVLLF TIQSKMRANN QKVYTPREGK LVNEINKAWE RLEKAEHERE LALRNELIRQ
EKLEQLARRF DRKAALRETW LSENQRLVTQ DNFGVDLPAV EAATKKHEAI EADIAAYEER
VQAVVDVARE LEAEDYHEVR RVCSRRDNVL RLWEYLQELL AARRHRLEAN LALQRVFQEM
LHIVDWMDEM KVRLLSQDYG KHLLGVEDLL QKHALVEADI TVQADRVKAV NAAAQRFSSE
DDAYKPCDSH VVSERATHLE ERYAELCSLA AERRSKLEES RKLWRFFWEM AELEGWVREK
EPLLSSGDVG KDLTGVLRLL GQHRAVEDEL NGRSADLKQT VREGEEMADA GHFGADDIRA
RVAEMHVLWA SLEDLAAQRK RRLQVAESLY QFQADADDIE VWMEDTLRIV SSDEMGHDEF
STQSLNKKHK DVTEEISSYR PVLDALHEQA QGLPDEVTVS AGVPDRLEAL EQRYRELVEL
SRVRKQRLQD ALALYKMYSE AEACELWIDE KSQWLNAMDV PEKLEDLEVI QHRFEGFEPE
MNSQASRIAV VNQLARQLMH AGHPSEQDIK AKQDHLNSVW SDFRELVDQK KEALSSALSI
QNFHLECNET KAWIREKTKV IESTQELGND LAGVMALQRK LSGMERDLAA IQTKLADLQG
EAERLASMHP EQEDAILGRL AEINQVWDNL KETLQNREES LGEASKLQQF LRDLDDFQTW
LSKAQTAIAS EDMPNTLPEA EKLLAQHEAI KNEIDNYQDD YQRMRDMGEV VTRDQSDPQY
MFLHQRLQAL DTGWNELNKM WENRHSLLSQ SHGFQAFLKD ARQADGFLSN QEYVLGHVEM
PATLESAEEA IKNHEDVMTT MDTNDEKIVG ALETGRRLLT EDNTYADKIQ EKVDSIDERH
KKNRMTAEDV LARLKDNRDL QRFLQDCQEL TLWINEKMLT AQDMSYDEAR NLHTKWQKHQ
AFMAELASNK EWLEKIDEEG QQLMVEKPET EPMVKEKLSE LHELWDELEN TTQLKAQRLF
DANRAELFTQ SCADLDKWVN QIESQISSDD HGNDLTSVNI LIKKQQMLEN QMEVRKKEVE
ELQSQATVLC QEGKGRDEVD SQRLTVENRF EQVLAPLQQR RDKLLASKEV HQYIRDLEDE
ILWVEERMPL AASRDHGNNL QTVQLLIKKN QNLQKEIQGH EPRIEDIRER GEDLIARGSV
DPEAIHERLE DLRALWATMI VEAKDRHIRL EESLKAQQYY FDVAEAEAWM SEQELYMIAD
EKAKDEQSAV AMLKKHQILE QSVENYSDVI HQLSETSRNL VTSRHPESER IGLRQSQADK
LYAGLKDLAE ERRGRLEERH KLFQLNREVD DLEQWIAERE VVAGSHELGQ DYEHVTMLSE
RFAEFARDTA TIGQERVDSV NRIADALIEA GHSDSASVAD WKDGLNEAWA DLLELIDTRT
QMLAASYELH RFNHDAREVL SRINEKQMQL PEELGRDQNT VESLQRKHTT FENDIQALGV
QVKVLQEDAE RLRGSYAGEK VEDIERREEE VVTAWKGLLD ACEARKLRLA DTGEKFRFFS
LVRDLMLWME NTIRQINAQE KPRDVSSVEL LMNNHQGIKA EIDTRNDNFT TVIELGKSLL
ARQHYATDEI KEKLGQLTDK RKEMVSKWEE RAHWLKLILE VHQFARDAGV AEAWLLAQEP
HITTQEVGES VDEVEQLLKR HEAFEKSVST WDERFNVLEK HTTLELLELR KQQEKEDEER
KQQKLQAELD EKKREEHHIA EQQRIQSQEV TQNGISSDQE SPRQGSNMLD PSVNGNGENE
ADGARKLTPE PSPSSDRRKP QTLHSQSVST LPGKAEEASA FRKEGFLLRK HEWESHNKKA
SSSVRSWHTL YCVLHNQEFG FYKDSKNMNT GNTYHNEIPV NLANAVCDVA SDYKKKKHVL
RLKLPDGNDY LLQAKDDEEM ANWIHSIKAA ASSRDSSSPS SQGSQAPMRS KTMPSGPPSE
ATSPEKKEKD REKRFSFLKM KK
//
