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Database: UniProt
Entry: A0A452RHF9_URSAM
LinkDB: A0A452RHF9_URSAM
Original site: A0A452RHF9_URSAM 
ID   A0A452RHF9_URSAM        Unreviewed;      2049 AA.
AC   A0A452RHF9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=SPTBN2 {ECO:0000313|Ensembl:ENSUAMP00000018344.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000018344.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000018344.1}
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; ENSUAMT00000020530.1; ENSUAMP00000018344.1; ENSUAMG00000005142.1.
DR   GeneTree; ENSGT00940000158847; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
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; cd21321; CH_SPTBN2_rpt2; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 6.
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:SF325; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 2; 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; 14.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 3.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 15.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 10.
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:UP000291022};
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          1883..1987
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1814..1879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1990..2049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          992..1019
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1098..1125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1855..1869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2028..2049
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2049 AA;  232434 MW;  5FFEBFF4C7A3450D CRC64;
     MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK
     KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG ETLPKPTKGR MRIHCLENVD
     KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD
     ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA
     FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
     MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
     EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
     EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
     VQAVDAVAAE LAAERYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL
     LYLMDWMEEM KGRLQSPDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP
     EYKPCDPQLV SERVASLERS YEALCKLAAA RRARLEESRR LWRFLWEVGE AEAWVREQQH
     LLASAETGRD LTGVLRLLNK HTALRGEMSG RLGPLKLTLE QGQQLVAEGH PGAGQAAART
     AELQAQWERL EALAEERAQR LAQAASLYQF QADANDMEAW LVDALRLVSS PELGHDEFST
     QALARQHRAL EEEIRSHRPA LDALREQAAA LPPALSHTPE VQGRVPSLER HYEQLQARAG
     ERARALEAAL ALYTMLSEAG ACGLWVEEKE QWLNGLALPE RLEDLEVVQQ RFETLEPEMN
     ALAARITAVN DIAEQLLKAK PPSRDSIVDT QKQLNHRWQQ FRTLADGKKA ALTSALSIQN
     YHLECTETQA WMREKTKVIE STQGLGNDLA GVLALQRKLA GTERDLEAIA ARVGELTREA
     NALAAGHPAQ APAINARLGE VQAGWEDLRA TMRRREESLG EARRLQDFLR SLDDFQAWLG
     RTQTSVASEE GPATLPEAEA LLAQHAALRG EVERARGEYS RLRALGEEVT RDQADPQCLF
     LRQRLEALGT GWEELGRMWE SRQGRLAQAH GFQGFLRDAR QAEGVLSSQE YVLSHTEMPG
     TLQAADAAIK NLEDFMSTMD ANGERIRGLL EAGRQLVSAG NIHAEKIQEK ADSIERRHKK
     NQEVVQQLLG RLRDNREQQH FLQDCHELKL WIDEKMLTAQ DVSYDEARNL HTKWQKHQAF
     MAELAANKDW LDKVDKEGRE LTLEKPELKA LVSEKLEDLH KRWDRLESTT QAKARSLFDA
     NRAELFAQSC SALESWLESL QAQLHSDDYG KDLTSVNILL KKQQVLCRCW NGRWLCERRR
     TSRAVEEKFR ALCQPMKERC RRLQASREQH QFHRDVEDEI LWVTERLPMA SSMEHGKDLP
     SVQLLMKKNQ TLQKEIQGHE PRIADLTERQ RALGAVAAGP ELAELQEMWK RLSRELELRG
     KRLEAALRAQ QFYRDAAEAE AWMGEQELHM MGQEKAKDEL SAQAEVKKHQ GLEQALADYA
     QTVHQLAASS QDMIDHDHPE STRISIRQAQ VDKLYASLKE LAGERRERLQ EHLRLCQLRR
     ELDDLEQWIQ EREVVAASHE LGQDYEHVTV SAGWTPAISE KLSQLQARRQ ETADKWQEKM
     DWLQLVLEVL VFGRDAGMAE AWLCSQEPLV RSAELGCTVD EVESLIKRHE AFQKSAVAWE
     ERFSALEKLT AVRAGGPQEC PPSPTAPGLC SPGSGTGDEA NGPRGEKQPR TRGPAPSVMP
     QSRSSESARV ATLPPRGPEL SAQEQMEGML CRKQEMEAFG KKAANRSWQN VYCVLRRGSL
     GFYKDAKAAS TGVPYHGEVP VSLARAQGSV AFDYRKRKHV FNCLRAPASQ QPCEMSSWLR
     VVNAAIATAS SASGEPEEPA VPSATRGMTR AMTMPPVSPV GAEGPVVLRS KDGREREREK
     RFSFFKKSK
//
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