ID A0A3B3S7J6_9TELE Unreviewed; 2161 AA.
AC A0A3B3S7J6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
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:ENSPKIP00000026448.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000026448.1}
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; ENSPKIT00000007204.1; ENSPKIP00000026448.1; ENSPKIG00000008760.1.
DR GeneTree; ENSGT00940000158908; -.
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: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; cd00176; SPEC; 9.
DR Gene3D; 1.20.58.60; -; 12.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF248; SPECTRIN BETA CHAIN, ERYTHROCYTIC; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 2.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 12.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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|PIRNR:PIRNR002297};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 54..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 172..277
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 2141..2161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1420..1461
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1628..1655
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2161 AA; 250354 MW; ED33ABAF26475ECC CRC64;
MTSTTDYDNV EITQQYSHVN MRFELSDEEL DNDHSSARRF ERSRIKALAD EREVVQKKTF
TKWVNSILSR VNCRISDLYH DLRDGRMLIK LLEVLSGEYL PKPTKGRMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLILGLI WTIILRFQIQ DIVVQADHKE TRSAKDALLL
WCQMKTAGYP NVNITNFTTS WKDGMAFNAL IHKHRPDVVD YPKLKVSNPI HNLQQAFNVA
EQKLGITKLL DPEDVFTENP DEKSIITYVV AFYHYFSKMK ALAVEGKRAG KVLDSAIETE
KMIHKYESLT SDLLTWIEQT IIVLNNRKLA NSLTGVQQQL QAFNSYRTVE KPPKFQEKGN
LEVLLFTIQS RMRANNQRVY TPREGALVAD INRAWERLER AENERERVLR EELIRQEKLE
QMARRFDRKA AMRETWLIEN QRLVSQDNFG YDLPAVEAAK KKHDAIETDI KAYQERVQGL
VAMSQALESA GYHDTKRIDA RKDNILRLWD YLQELLIARR GRLEKNLTLQ KIFQEMLHVI
SWMDEVKTRL LSPDFGKHLL EVEDLLQKHA LVEADIAMQA ERVSSASAAA LKFANGDSYK
PCDPQVIRDR VQHLELCYQE LCALAAQRKA RLHQSRRLWN FFWETAELES WIKEKEHIFS
SMDYGKDLTG VLVLQNKHNA FEDELGARRA HLQQVMDEGD KMVQARHFGT PGIQQRMADV
HRQWQQLEDL AAFRKRNLQD TQKFFQIQGD ADDLKTCLLD GRRQMMSSDL GHDEYTTQRL
FRKHRSLQDE LTKNAATIDT LFKQANSLPE ELRNTPDIQR RLTDIRDLYM ELLSLSDLRK
KKLEDAMALY TIFSESDACE LWMSQKETWL VGLETPEKLE DLEVVQNRLS ILAQEMGNVQ
SRVDGVNNAA QQLEDSRHPS MKEVKECQAH LNNRWDAFKA MVEDKKQRVD SALSLHNYGL
ECDETKAWIK DKTRVIESTQ DLGNDLAAVM TIQRKLYGME RDLAAIEDKL VFLQGEASLL
AKDHPENADD IFGRLQTLGQ AWDELKATLK GREESLGEVS KLQTFLQDLD DFQSWLFKTQ
KAIASDEMPT TLPEAEQLLD LHAAAQTDMY NHEEDYHRLK DTGITVTQDK TDPQYQQLEQ
RLKGLDTGWG ELHKIWDSRK NFLEQGLGFQ QFMRDAKQSE AILNNQEYTL AHAEHPDTLD
GAEQVLRKHE DFVTTMDANR EKILNTLEGG QKLVESGNLY SERIKNKMES IEDRYNTNQG
KAREVSQKLK DNRDLQHFLQ NTQDLTLWIN EKMLTAQDAS YDEARNLHSK WQKHQAFMAE
LASNKDWLNK IDQEGHELMQ AKPEFEPVVK ERLLKLHKLW NELESTTQEK ARLLFDANRS
ELFDQSLSDL KNWLTVLQQQ LQADEDVKDL ISANILLKKH QMTENQIRDR GRELEELQEA
VQSMREDRPG MEVELQTLQQ QFQHVLTPLA ERRGKLEASM AVHQFFRDLA DEILWVEERL
PLATSEEHGN NLQSVQMLLK KNQTLQKEID GHQPRIDEIL ERGSRMRAAE SPKPVRIEEQ
MKELQDMWTR LQEETSKRRD RLNASKLAQQ YYNDADEAEA WTGEQELYMI ADEMAKDEQN
AALLLKRHST LKQNVDEYAE SIQQLADRAQ KMLAEDHPDG EAIIRRQGQV DKQYASLKDL
AEERKKKLDH TCHHFQLCRE VEDLEQWIAE RDVVASSQEM GQDLDHVTIL RDKFREFARE
TGTHGQERVD AFNQIIDVLI EAGHSEAATM AEWKDSINES WADLLELIDT RAQLLTASYD
LLKYFYDGKE LVAQIREKQT QLPDDVGEDF SKAESFHRMH AAFERDISTL GKQVQQFQET
ATRLRAQYAG EQATAIQTTE REVVEAWKTL LDACDGRRSH LVDTADKFRF FTTVRDLLAW
MESIIQQIET QEKPRDVSSV ELLMKYHQGI RSEIDTRNPK YNACVELGRS LLVRQHRDSA
EVRFLKVTGQ SCFEYESCES RWGLITIVLL EVCQFARDAS VAEAWLIAQE PHVVSKEVGQ
TVDEVEKLLK RHEAFEKSSA TWEERFAALE RLTTVRFAPV EPSPSQREGS AEDTTAAVVL
EVDESSPGEE LQKLTKETKE AATLPAGAPK GQAVILEGTL GRKHELEATG KKASNRSEFR
F
//
