ID A0A2K6GWC7_PROCO Unreviewed; 2387 AA.
AC A0A2K6GWC7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN2 {ECO:0000313|Ensembl:ENSPCOP00000030537.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000030537.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000030537.1}
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; ENSPCOT00000041485.1; ENSPCOP00000030537.1; ENSPCOG00000027979.1.
DR GeneTree; ENSGT00940000158847; -.
DR OMA; DNHEPWI; -.
DR Proteomes; UP000233160; 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: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; 8.
DR Gene3D; 1.20.58.60; -; 13.
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; 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; 17.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 12.
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:UP000233160};
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 2223..2325
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2080..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2156..2227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2328..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 994..1021
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1100..1127
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1425..1452
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2080..2100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2115..2140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2191..2211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2366..2387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2387 AA; 270167 MW; FFD87D43EB0B5F56 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 IEQMIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
VQAVDAVAAE LAAEHYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL
FYLMDWMEEM KGRLQSQDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP
EKEYRPCDPQ LVSERVATLE QSYEALCKLA ATRRARLEES RRLWRFLWEV GEAEAWVREQ
QHLLASAETG RDLTGVLRLL NKHTALRGEM SGRLGPLRLT LEQGQQLVAE GHPGAGQAAA
RAAELQAQWE RLEALAEERA QRLSQAASLY QFQADANDME AWLVDALRLV SSSELGHDEF
STQALARQHR ALEEEIRGHR PTLDALREQA AALPLALSRT PEVQGRVPTL ERHYQALQAQ
AGERAQALEA ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
MNALAARITA VNDIAEQLLK ANPPGKDRIV NTQKQLNHRW QQFRSLADGK KAALTSALSI
QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTERDLEA IAARVGELTR
EANALAAGHP AQAPAINARL GEVQAGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGLQGFLRD ARQAEGVLSS QEYVLSHTEM
PGTLQAADAA IKKLEDFMST MDASGERIRG LLEAGRQLVS EGNIHAEKIR DKADSIERRH
RKNQEAAQQL LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ
AFMAELAANK DWLDKVDKEG RELTLEKPEL KALVSEKLGD LHRRWDELET TTQAKARSLF
DANRAELFAQ SCSALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLER EMAVREKEVE
AIQAQAKALA QEDQGAGEVE RTSRAVEEKF RALYQPMQER CQRLQASREQ HQFHRDVEDE
ILWVTERLPM ASSVEHGKDL PSVQLLMKKN QTLQKEMQGH EPRIADLTAR QRALGAAAAG
PELAELQGLW KRLGRELELR GKRLEEALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE
PSAQAEVKKH QVLEQALANY ARTVHQLAAS SQDLIDHDHP ESTRISIRQA QVDKLYASLK
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSAQVQQVQ
DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM
LWMDGVNLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG QELLARSHYA
AEEISEKLSQ LRARRQETAD KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE
LGCTVDEVES LIKRHEAFQK SAVAWEERFS ALEKLTALEE REKEQRRKRE EEERRKQPPA
PEPRASLPQG GLVDGQTAPD TTWDGTQPRL PPSAQAPSIN GVCTDAEASQ PLLEQQRLEQ
SSFPEGPVSS LDGPSVGEEA GGPRGERQTR TRGPAPQTMP QSRSSESTHV ATLPPRGPEP
SAQEQMEGML CRKQEMEAFG KKAANRSWQN IYCVLRRGSL GFYKDAKAAS TGVPYHGEVP
VSLARAQGSV ASDYRKRKHV FKLGCLSVLQ AEMSSWLRVV NAAIATASSA SGEPEEPAAP
GAPRGMTRAM TMPPVAPAGA EAPVVLRSKD GREREREKRF SFFKKNK
//
