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Database: UniProt
Entry: A0A2R9CD50_PANPA
LinkDB: A0A2R9CD50_PANPA
Original site: A0A2R9CD50_PANPA 
ID   A0A2R9CD50_PANPA        Unreviewed;      2397 AA.
AC   A0A2R9CD50;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   Name=SPTBN4 {ECO:0000313|Ensembl:ENSPPAP00000039871.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000039871.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000039871.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000039871.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AJFE02039786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02039795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPPAT00000062783.1; ENSPPAP00000039871.1; ENSPPAG00000042534.1.
DR   GeneTree; ENSGT00940000156343; -.
DR   Proteomes; UP000240080; Chromosome 19.
DR   Bgee; ENSPPAG00000042534; Expressed in cerebellum and 5 other cell types or tissues.
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; cd21322; CH_SPTBN4_rpt2; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 6.
DR   Gene3D; 1.20.58.60; -; 11.
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:SF232; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 4; 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; 2.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..103
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          118..223
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2251..2360
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          615..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2027..2266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2366..2397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          402..436
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1288..1315
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1501..1528
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2065..2151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2201..2227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2397 AA;  270698 MW;  AB8E78104180F130 CRC64;
     QKKTFTKWVN SHLARVGCHI GDLYVDLRDG FVLTRLLEVL SGEQLPRPTR GRMRIHSLEN
     VDKALQFLKE QRVHLENVGS HDIVDGNHRL TLGLVWTIIL RFQIQVIKIE TEDNRETRSA
     KDALLLWCQM KTAGYPEVNI QNFTTSWRDG LAFNALIHRH RPDLVDFSKL TKSNANYNLQ
     RAFRTAEQHL GLARLLDPED VNMEAPDEKS IITYVVSFYH YFSKMKALAV EGKRIGKVLD
     QVLEVGKIIE RYEELAAELL AWIHRTVGLI SNQKFANSLS GVQQQLQAFT AYCTLEKPVK
     FQEKGNLEVL LFSIQSKLRA CNRRLFVPRE GCGIWDIDKA WGELEKAEHE REAALRAELI
     RQEKLELLAQ RFDHKVAMRE SWLNENQRLV SQDNFGYELP AVEAAMKKHE AIEADIAAYE
     ERVQGVAELA QALAAEGYYD IRRVAAQRDS VLRQWALLTG LVGARRTRLE QNLALQKVFQ
     EMVYMVDWME EMQAQLLSRE CGQHLVEADD LLQKHGLLEG DIAAQSERVE ALNAAALRFS
     QLQGYQPCDP QVICNRVNHV HGCLAELQEQ AARRRAELEA SRSLWALLQE LEEAESWARD
     KERLLEAAGG GGAAGAAGAA GTAGGAHDLS STARPPRPSN KILRGRAWAG GGVAAAGPAV
     HRAPVGLAER AASARRRWQR LEEAAARRER RLQEARALHQ FGADLDGLLD WLRDAYRLAA
     AGDFGHDEAS SRRLARQHRA LTGEVEAHRG PVSGLRRHGA GPLVVALQVR VVEAEQLFAE
     VTEVAALRRQ WLRDALAVYR MFGEVHACEL WIGEKEQWLL SMRVPDSLDD VEVVQHRFES
     LDQEMNSLMG RVLDVNRTVQ ELVEGGHPSS DEVRSCQDHL NSRWNRIVEL VEQRKEEMSA
     VLLVENHVLE VAEVRAQVRX XXXXXXVAAA GRLQRFLHDL DAFLDWLVRA QEAAGGSEGP
     LPNSLEEADA LLARHAALKE EVDQREEDYA RIVAASEALL AADGAELGPG LALDEWLPHL
     ELGWHKLLGL WEARREALVQ AHIYQLFLRD LRQALVVLRN QEMALSGAEL PGTVESVEEA
     LKQHRDFLTT MELSQQKMQV AVQAAEGLLR QGNIYGEQAQ EAVTRLLEKN QENQLRAQQW
     MQKLHDQLEL QHFLRDCHEL DGWIHEKMLM ARDGTREDSH KLHKRWLRHQ AFMAELAQNK
     EWLEKIEREG QQLMQEKPEL AASVRKKLGE IRQCWAELES TTQAKARQLF EASKADQLVQ
     SFAELDKKLL HMESQLQDVD PGGDLATVNS QLKKLQSMES QVEEWYREVG ELQAQTAALP
     LEPASKELVG ERQNAVGERL VRLLEPLQER RRLLLASKEL HQVAHDLDDE LVRPAQGPGG
     LGTPPLHPHP LTSCPQGLRR EIQAHGPRLE EVLERAGALA SLRSPEAEAV RRGLEQLQSA
     WAGLREAAER RQQVLDAAFQ VEQYYFDVAE VEAWLGEQEL LMMSEDKGKD EQSTLQLLKK
     HLQLEQGVEN YEESIAQLSR QCRALLEMGA PGQQISRRQS QVDRLYVALK ELGEERRVAL
     EQQYWLYQLS RQVSELEHWI AEKEVVAGSP ELGQDFEHVS VLQEKFSEFA SETGTAGRER
     LAAVNQMVDE LIECGHTAAA TMAEWKDGLN EAWAELLELM GTRAQLLAAS RELHKFFSDA
     RELQGQIEEK RRRLPRLTTP PEPRPSASSM QRTLRAFEHD LQLLVSQVRQ LQEGAAQLRT
     VYAGEHAEAI ASREQEVLQG WKELLSACED ARLHVSSTAD ALRFHSQVRD LLSWMDGIAS
     QIGAADKPRD VSSVEVLMNY HQGLKTELEA RVPELTTCQE LGRSLLLNKS AMADEIQAQL
     DKLGTRKEEV SEKWDRHWEW LQQMLEVHQF AQEAVVADAW LTAQEPLLQS RELGSSVDEV
     EQLIRRHEAF RKAAAAWEER FSSLRRLTTI EKIKAEQSKQ PPTPLLGRKF FGDPTELAAK
     AAPLLRPGGY ERGLEPLARR ASDTLSAEVR TRVGYVRQEL KPERLQPRID RLPEIPGRVE
     PAALPAAPED AAETPVTPAA AEQVRPRPER QESADRAEEL PRRRRPERQE SVDQSEEAAR
     RRRPERQESA EHEAAHSLTL GRYEQMERRR ERRERRLERQ ESSEQEMPIR GDLVKGKATL
     ADIVEQLQEK EAGPGLPAGP SLPQPRELPP GRLPNGLELP ERTPRPDRPR GAGPAKPRRR
     EGGEGGGSRR SRSAPAQGGS APAPPPPPTH TVQHEGFLLR KRELDANRKS SNRSWVSLYC
     VLSKGELGFY KDSKGPASGS THGGEPLLSL HKATSEVASD YKKKKHVFKL QTQDGSEFLL
     QAKDEEEMNG WLEAVASSVA EHAEIARWGQ TLPTTSSTDE GNPKRESGDR RASGRRK
//
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