ID A0A3B3QD35_9TELE Unreviewed; 2352 AA.
AC A0A3B3QD35;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSPKIP00000004063.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000004063.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000004063.1}
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; ENSPKIT00000028035.1; ENSPKIP00000004063.1; ENSPKIG00000021235.1.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000261540; 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; cd21246; CH_SPTB-like_rpt1; 1.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 9.
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; 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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 49..153
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 168..273
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2177..2287
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2084..2178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2289..2352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..486
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 986..1020
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1089..1119
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1417..1444
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2107..2124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2289..2320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2321..2345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2352 AA; 271969 MW; 6699B17A623C1C90 CRC64;
MELQRAASVS GPLSPGPGPS PVLGYSAQAA FNYNQLEGRF KQLQDEREAV QKKTFTKWVN
SHLARVSCRI TDLYMDLRDG RMLIKLLEVL SGERLPKPTK GRMRIHCLEN VDKALQFLKE
QRVHLENMGS HDIVDGNHRL TLGLIWTIIL RFQIQDISVE TEDNKEKKSA KDALLLWCQM
KTAGYPNVNI HNFTTSWRDG MAFNALIHKH RPDLIDFDKL KKSNAHYNLQ NAFNLAEQHL
GLTKLLDPED ISVDHPDEKS IITYVVTYYH YFSKMKALKV EGKRIGKVLD NAIETEKMIE
KYESLASDLL EWIEQTIIIL NNRKFANSLV GVQQQLQAFN TYRTVEKPPK FTEKGNLEVL
LFTIQSKMRA NNQKVYMPRE GKLISDINKA WERLEKAEHE RELALRTELI RQEKLEQLAR
RFDRKAAMRE TWLSENQRLV SQDNFGFDLQ AVEAATKKHE AIETDIAAYE ERVQAVVAVA
RELEAENYHD IKRITARKDN VIRLWEYLLE LLRARRSRLE MNLGLQKVFQ EMLYIMDWMD
EMKMLLLSQD YGKHLLGVED LLQKHALVEA DIGIQADRVK NVNANAQKFA LDTEGYKPCD
PQVIRDRVAH MEFCYQELTQ LAAERRARLE ESRRLWKFFW EMAEEEGWMR EKEQILSSED
CGKDLTAAIR LLSKHRAFED EMSGRSGRLQ QSVREGEAMV EAQHFGSDKI RERTTDIREQ
WAALGRLAAV RRTRLEEALS LHQFQVDADD IDTWMLDVLR IVSSADVGHD EFSTQALVKK
HKDVAEETAS YRPIIDALRE QSCALPGEHG QSEEVQSRLA GIEERYREVA ELTRLRKQAL
QDALALYKMS SEADACELWI DEKEQWLNSM QIPEKLEDLE VIQHRFESLE PEMNNQASRV
AVVNQIARQL VHSGHPGEKE IKAQQDKLNT RWSQFRDLVD LKKDALNSAL GVQNYHLECN
ETKSWIREKT KVIESTQELG NDLAGVMALQ RKLTGMERDL VAIEDKLTDL QKEAERLAAE
HPDQAQAIMG RLAEITGVWE EMKTTLRNRE ESLGEASKLQ QFLRDLDDFQ SWLSRTQTAI
ASEDMPNTLA EAEKLLTQHE NIKNEINNYE EDYQKMRDMG EMVTQGQTDA QYMFLRQRLQ
ALDTGWNELH KMWENRQSLL SQSHAYQLFL RDTKQAEAFL NNQEYVLAHT EMPTTLEAAE
GAIKKQEDFM TTMDANEEKI NAVVETGRRL VSDGNINSER IQERVDSIDD RHKKNREAAS
ELLMRLKDNR DLQKFLQDCQ ELSLWINEKM LTAQDMSYDE ARNLHSKWLK HQAFMAELQS
NKEWLDKIEK DGTQLVAEKP ETQAVVKEKL SSLHSMWNDL ESTTQTKAQC LFDANKAELF
SQSCADLDKW LVGLDGQIHS DDYGKDLTSV NILLKKQQML ENQVEVRRKE VEELQSQAQA
LSQEGKDSDE VDGRRRGVEH KFQKMLDPLH KRKDNLMASK EIHQFNRDVE DEILWVEERM
PLATSTDHGH NLQTVQLLIK KNQTLQKEVQ GHQPRFNDIF ERSQSILKDD SPTAEAIRQR
LADLRQLWDQ MIQETENRHS RLEEAHKAQQ YYFDAAEAEA WMSEQELYMM SEEKAKDEQS
AVAMLKKHQI LEQAVEDYAE TVHQLSKTSR ALVAAGHPES ERINMRQSQV DKLYAGLKDL
SEERRGKLDE RFRLFQLNRE VDDLEQWIAE REVVAGSHEL GQDYEHVTML QERFREFARD
TGNIGQERVD AVNQMADDLI NSGHSDAATI AEWKDGLNEA WADLLELIDT RTQILAASFE
LHKFYHDAKE ILGRILDKHK KLPEELGRDQ NTVETLQRMH TTFEHDIQAL GTQVRQLQED
AVRLQSAYAG DKADDIQKRE SEVLETWKSL LEACEGRRVR LLDTGDKFRF FSMVRDLMLW
MEDVIRLIEA QEKPRDVSSV ELLMNNHQGI KAEIDARNDS FTTCIELGKA LLARKHYASD
EIKEKLVQLT DKRKDMIDKW EDRWEWLRLV LEVHQFSRDA GVAETWLLAQ EPYLSSREMG
QSVDEVEKLI KRHEAFEKSA ATWEERFSAL ERLTTMELLE VRRQQEEEER RRQPLSPEAL
PAPDSDSQQR EGEQASQNGL PSDQDSPRDG VDGADMVNGV AERSSKEPSP APSPSAERKG
RSSQAATLPA KAQDSPSAQL EGFLHRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDS
KTASQGIPYH SEIPISLKDA VCEVALDYKK KKHVFKLRIS DGNEYLFQAK DDEEMNTWIQ
AITSAVTSAA TSDVTPSSQS TPASSRAQTL PTGVSLTTES SPGKKEKEKD KEKEKEKEKE
KEKRFSLFSK KK
//
