ID A0A096NVL3_PAPAN Unreviewed; 2236 AA.
AC A0A096NVL3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTB {ECO:0000313|Ensembl:ENSPANP00000017088.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000017088.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000017088.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000017088.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 9555.ENSPANP00000017088; -.
DR Ensembl; ENSPANT00000013648.3; ENSPANP00000017088.2; ENSPANG00000017505.3.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000158908; -.
DR HOGENOM; CLU_000146_1_2_1; -.
DR OMA; EPADMTS; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000028761; Chromosome 7.
DR Bgee; ENSPANG00000017505; Expressed in skeletal muscle tissue and 49 other cell types or tissues.
DR ExpressionAtlas; A0A096NVL3; baseline.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProt.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
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 GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
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: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; 1.
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; 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:UP000028761};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..68
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 81..186
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2086..2196
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1982..2057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..406
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 905..932
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1446..1480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1982..1999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2236 AA; 257142 MW; 103A2C983868C580 CRC64;
MPTGATAVPQ PKPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDVVD GNHRLVLGLI
WTIILRFQIQ DIVVPTQEGR ETAKDALLLW CQMKTAGYPH VNVTNFTSSW KDGLAFNALI
HKHRPDLIDF DKLKDSNARH NLEHAFDVAE RQLGIIPLLD PEDVFTENPD EKSIITYVVA
FYHYFSKMKV LAVEGKRVGK VIDHAIETEK MIEKYSGLAS DLLTWIEQTI TVLNSRKFAN
SLTGVQQQLQ AFSTYRTVEK PPKFQEKGNL EVLLFTIQSR MRANNQKVYT PHDGKLVSDI
NRAWESLEEA EYRRELALRN ELIRQEKLEQ LARRFDRKAA MRETWLNENQ RLVAQDNFGY
DLAAVEAAKK KHEAIETDTA AYEERVRALE DLAQELEKEN YHDQKRITAR KDNILRLWSY
LQELLRSRRQ RLETTLALQK LFQDMLHSID WMDEIKAHLL SAEFGKHLLE VEDLLQKHKL
MEADIAIQGD KVKAITAATL KFTEGKGYQP CDPQVIQDRI SHLEQCFEEL SNMAAGRKAQ
LEQSKRLWKF FWEMNEAESW IKEKEQIYSS LDCGKDLTSV LILQRKHKAF EDELRGLDAH
LEQIFQEAHD MVARKQFGHP QIEARIKEVS AQWDQLKELA AFRKKNLQDA ENFFQFQGDA
DDLKVWLQDA HRLLSGEDVG QDEGATRALG KKHKDFLEEL EESRGVMEHL EQQAQGFPEE
FRDSPDVTHR LQALRELYQQ VVAQADLRQQ RLQEALDLYT VFGETDACEL WMGEKEKWLA
EMEMPDTLED LEVVQHRFDI LDQEMKTLMT QIDGVNLAAN SLVESGHPRS GEVKQYQDHL
NTRWQAFQTL VSKRREAVDS ALRVHNYCVD CEETSKWITD KTKVVESTKD LGRDLAGVIA
IQRKLSGLER DVAAIQARVD ALERESQQLM DSHPEQKEDI GQRQKHLEEL WQGLQQALRG
QEDLLGEVSQ LQAFLQDLDD FQAWLSITQK VVASEDMPES LPEAEQLLQQ HAGIKDEIDG
HQDSYQRVKE SGEKVIQGQT DPEYLLLGQR LEGLDTGWDA LGRMWESRSH TLAQCLGFQE
FQKDAKQAEA ILSNQEYTLA HLEPPDSLEA AEAGIRKFED FLGSMENNRD KVLSPVDSGN
KLVAEGNLYS DKIKEKVQLI EDRHRKNNEK AEEASVLLRD NLELQNFLQN CQELTLWIND
KLLTSQDVSY DEARNLHNKW LKHQAFVAEL ASHEGCLENI DAEGKQLMDE KPQFTALVSQ
KLEALHRLWD ELQATTKEKT QHLSAARSSD LRLQTHADLN KWISAMEDQL RSDDPGKDLT
SVNRMLAKLK RVEDQVNVRK EELGELFAQV PSTGEEAGDV DLSIEKRFLD LLEPLGRRKK
QLESSRAKLQ INRDVEDETL WVEERLPLAQ STDYGTNLQT VQLFMKKNQT LQNEILGHTP
RVEDVLQRGQ QLVEAAEIDC QDLEERLRHL QSSWDRLQEA AAGRLQRLRD ANEAQQYYLD
ADEAEAWIGE QELYVISDEM PKDEEGAIVM LKRHLRQQRA VEDYGRNIKQ LASRAQGLLS
AGHPEGEQII RLQGQVDKHY AGLKDVAEER KRKLENMYHL FQLKRETDDL EQWISEKELV
ASSPEMGQDF DHVTLLRDKF RDFARETGAI GQERVDNVNA FIERLIDAGH SEAATIAEWK
DGLNEMWADL LELIDTRMQL LAASYDLHRY FYTGAEILGL IDEKHRELPE DVGLDASTAE
SFHRVHTAFE RELHLLGVQV QQFQDVATRL QTAYAGEKAE AIQNKEQEVS AMWQALLDAC
AGRRTQLVDT ADKFRFFSMA RDLLSWMESI IRQIETQERP RDVSSVELLM KYHQGINAEI
ETRSKNFSAC LELGESLLQR QHQASEEIRE KLQQVMSRRK EMNEKWEARW ERLRMLLEVC
QFSRDASVAE AWLIAQEPYL ASGDFGHTVD SVEKLIKRHE AFEKSTASWA ERFAALEKPT
TLELKERQIA ERPAEETGPQ EEEGETAGEA PVSHHAATER TSPGEEEGTW PQNLQQPPPP
GQHEDGQKSA GDERPTTEPL FKVLDTPLSE GDEPATLLAP RDHGHSVQME GYLGRKHDLE
GPNKKASNRS WNNLYCVLRN SELTFYKDAK NLALGMPYHG EEPLALRHAI CEIAANYKKK
KHVFKLRLSN GSEWLFHGKD EEEMLSWLQG VSTAINESQS IRVKAQSLPL PSLSGPDPSL
GKKDKEKRFS FFPKKK
//
