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Database: UniProt
Entry: A0A1S3SR21_SALSA
LinkDB: A0A1S3SR21_SALSA
Original site: A0A1S3SR21_SALSA 
ID   A0A1S3SR21_SALSA        Unreviewed;      2376 AA.
AC   A0A1S3SR21;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=LOC106611276 {ECO:0000313|RefSeq:XP_014066789.1,
GN   ECO:0000313|RefSeq:XP_014066790.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014066789.1};
RN   [1] {ECO:0000313|RefSeq:XP_014066789.1, ECO:0000313|RefSeq:XP_014066790.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014066789.1,
RC   ECO:0000313|RefSeq:XP_014066790.1};
RG   RefSeq;
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   RefSeq; XP_014066789.1; XM_014211314.1.
DR   RefSeq; XP_014066790.1; XM_014211315.1.
DR   STRING; 8030.ENSSSAP00000062123; -.
DR   PaxDb; 8030-ENSSSAP00000062123; -.
DR   GeneID; 106611276; -.
DR   KEGG; sasa:106611276; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
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; 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:SF248; SPECTRIN BETA CHAIN, ERYTHROCYTIC; 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; 16.
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|PIRNR:PIRNR002297};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR002297};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          54..158
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          177..282
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2213..2323
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1446..1466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2326..2376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          461..495
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1001..1028
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1570..1597
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2356..2376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2376 AA;  274429 MW;  D942C8C20425D1D9 CRC64;
     MTSTTDFDNV EITQQYSRIN TRFELLGEEL DNDNSSARLF ERSRIKALAD EREAVQKKTF
     TKWVNSILCR VSCRISDLYL DLRDGRMLIK LLELLSGEKL PKPTKGRMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLILGLI WTIILRFQIQ DIVVEMGQVD GTQRQSRTAK
     DALLLWCQMK TAGYPNVNIT NFTTSWKDGM AFSALIHKHR PDLVDYSGLK RSNPTHNLQN
     AFNVAEQTLG VTKLLDPEDV FTENPDEKSI ITYVVAFYHY FSKMKALAVE GKRVGKVLDH
     AIETEKMIDK YETLSSDLLT WIQQTIIVLN NRKLANSLTG VQQQLQSFNS YRIVEKPPKF
     QEKGNLEVLL FTIQSRMRAN NQRVYTPKEG ALVADLNRAW EHLERAEHER ERVLRDELIR
     QEKLEQMARR FDRKASMRET WLLENQRLVA QDNFGYDLPA VEAAKKKHDA IETDIAAYEE
     RIQGIVAISN ELESERYHDT KRIDVRKDNI LRLWDYLQEL LKARRTRLDK NLTLQRIFQE
     MLYIITWMDG MKARLLSPDF GKHLLEVDDL LQKHALVEAD ITVQAERVHD SNVAALKFAN
     GDSYKPCDPQ VIKDRVQHLD LCYQELCALA AQRRARLEQS RRLWNFFWEM AELESWIKEK
     EHIFSSLDYG KDLTSVLVLQ SKHSAFENEL GARRAHLQEI MDEGDKMIQS RHFGAPQVGD
     CMEDVRRQWQ QLEELAAFRR QNLQDTQRFF QLQGDAEDLK AGLLDAKRQM TSDDMGHDEY
     TTQRLLKRHR DLRNDVAKNG ATIDALTKQA AMLPEELRNT PDIQRRLKDI RDMYMELMSL
     CDLRQKKLDD AMALYTIFSE TDSCELWMGQ KETWLVGLDV PENLEDLEVV QNRLSILASD
     MANVQTRVDD VNKAVKQLED SRHPCTKEVK ECQLRLNTRW EAFKAMVEDK KRKVDSALSY
     HNYGLECDET EAWIRDKTRV IKSTQDLGND LNAVMTIQRK LYGMERDLAA IEDKLNFLRS
     EADQLAKDHP DNAADILSRR AELDAAWDNL RATLKDREDS LGEVSKLQTF LQDMDDFQSW
     LFKTQKAVAS EDMPETLPQA EQLLNLHDDV YDDMDAHEED YHKVRDTGVA VTQGQLDDPQ
     YQELDKRLKG LDRGWDELHK MWDSRKGFLD QGLGFQLFMR DTKQVETILN NQEYTLAHTD
     KHDTLDGAEH ALKKHEDFVC TMDANMEKLA STLEGGQRLV DSGNLYSPRV QDKMDSIYDR
     YNKNRGKANE VTGILKDNRD LQHFLQNTQD LTLWINEKML TAQDVSYDGD RNLHTKWKKH
     QAFMAELASN KDWLNKIDQE GQELMDSKPD FEPIVTVRLA KLHELWDKLE STAEDKACLL
     FDANRSELFD QSQADMKKWL AELQKELQGD DEVKDLTNAN ILLKKHQQTE NHVRDRAREL
     EDLQEAVQKH GGPAGSREDQ PELEAEQQAI QRDFQQLLTP LAQRRGKLEA AKAVHQFYRD
     LADEILWVEE RLPLAMSDEH GSNLQTVQLL LKKNQTLQRE MKGHQPRVNE VLERGRRMAS
     AATEEGGPEA ERIGEQVKEL KEVWARLQEE MAKRRDRLNG SNRAQQYYND ADEAEAWIGE
     QELYMIADDK AKDEQSAMLM LKRHLIVKQA VDDYSDSIQK LSDRAQKMLN EDHPNGESII
     RRQGQVDKQY AGLKDLAEER RRKLDHVYHH FLLSREVEDL EHWIAERDVV ASSQEMGQDL
     DHVTILRDKF RDFSRETGMV GQERVDYVNQ TIDELIKAGH TEAAAMADWR DSVNESWADL
     LELVDTRAQL LQASHDLLKY FDDGKELVSQ IQEKLNEIPA DLGEDFSKAD TFHRMHAAFE
     RDISALGKQV QQFQETAACL HAQYAGDKAT EIQAQEKEVV EAWKALLDAC DGRRKRLEET
     ADKFRFFTMV RDLMAWMEST IQQIETQEKP RDVSSVELLM KYHQGIRSEI DQRGPKFSDC
     VAHGKALLAR KHKYSAEIKE KLIQLMEKKK EMMTKWDDRW DWLRLLLEVC QFARDASVAE
     AWLVAQEPYV ASKDLGQTVN EVEKLLKRHE AFEKSTATWE ERFSALERLT TLELLELRKQ
     QQEIQQFVTE EQKPSQMESR REDTGFAEDS SQLYTIEEQT LSASGAVEVE PSLGQLEGTA
     GDSTVPMVSE MQDAGLQEAS SLELLDASVS GHTPREREPR AATLPADPLS PKAVLQEGML
     GRKHDLEAAG KKASNRSWNN LYCVLKPGQL SVYKDAKSFG HGSNYHGEGP LSLSNAKWEV
     LNNYKKKKHV FILRLGDGSE YLFQCKDEEE LGCWTQAMEK AVKPLAQEEV EPSGSAGVRA
     RSLPPPSSST TLTTPEPAKD KKDKEKKGFS RFANKK
//
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