ID A0A2K6EQ37_PROCO Unreviewed; 2106 AA.
AC A0A2K6EQ37;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTB {ECO:0000313|Ensembl:ENSPCOP00000003848.1};
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:ENSPCOP00000003848.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000003848.1}
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; ENSPCOT00000013044.1; ENSPCOP00000003848.1; ENSPCOG00000011451.1.
DR GeneTree; ENSGT00940000158908; -.
DR OMA; EPADMTS; -.
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:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR CDD; cd21319; CH_SPTB_rpt2; 1.
DR CDD; cd21317; CH_SPTBN2_rpt1; 1.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.20.58.60; -; 12.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 13.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 54..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 173..278
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2069..2106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1538..1572
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2106 AA; 242998 MW; 643B3BF153CBFE60 CRC64;
MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF
TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVIETQEGQ ETRSAKDALL
LWCQMKTAGY PRVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV
AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
EKMIEKYSGL ASDLLTWIEQ TITVLNNRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG
NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYQRELAL RNELIRQEKL
EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA
LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLRSR RQRLETTLAL QKLFQDMLHS
IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVRAITAA TLQFAEEKGY
QPCDPQVIRD RISHLEQCFG ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY
SSLDYGKDLT SVLILQRKHK AFEDELRGLG THLEQIFQEA EGMIARKQFG HPQIKARITE
VSAQWDQLKE LAAFRKNNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA
LGKKHKDFLE ELEENRLVME HLEQQAQGFP QEFRDSPDVT NRLQALQEVY QQVVAQADLR
GQRLQDALDL YTVFGETDAC ELWMGEKEKW LAQMEIPDTL EDLEVVQHRF DILDQEMKTL
ITQIDGVNLA ANSLVESGHP RSGEVKQYQD HLNTRWQAFR TMVSARREAV DSALRVHNYC
VDCEETSKWI TDKTKVVEST KDLGRDLAGV IAIQRKLSGL ERDVAAIQAR VGVLERESQR
LMESHPELKE DISRRQAYVE ELWQGLQRAL QGQEASLGEA SQLQAFLQDL DDFQGWLSMT
QKAVASEDTP ESLPEAEQLL QQHAAIKDEI DGHQESYQHV KDSGEKVIRD QKDPEYVLLG
QRLRGLDSGW DALRRMWESR GHSLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL
EAAEAGIRKF EEFLVSMENN RDKVLSPVDS GNKLVAEGNL YSDKIREKVQ LIEDRHRKND
EKAQEASVVL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYGEARNLHN MWLKHQAFVA
ELASHQGWLE NIDAEGKQLM EEKPQYADLV SQRLDALHRL WDELQTTTKE KARQLSAARS
SDLRLQTHAD LSKWISAMED QLRSDDPGKD LTSVNRMLVK LKRVEDQVNV RKEELGELFA
QVPSLEEEVG DADVSIEKRF LDLLEPLERR KKQLESSKAK LQISRDLEDE TLWVEERLPL
AQSADYGTNL QTVQLFMKKN QTLQNEIQGH APRVEDVLQR GQQLVAAAEI DCEDLEERLG
HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDAGEAEAWI GEQELYVIST ETPEDEEGAI
VMLKRHLRQQ RAVEEYGRNI KQLAGRAQGL LSAGHPEGEQ IIRLQGQVDK QYARLKDTAE
TRKRKLEDEY HLFQLKRETE DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG
AIGQERVDNM NAIIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH
RYFYTGTEIL GLIGEKHREL PEDVGLDAST AESFHWVHTA FERELHLLGM QVQQFQDVAT
RLQTAYAAEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME
SIIRQIETQE RPRDVSSVEL LMKYHQGISA EIETRSKNFS ACLELGESLL QRQHQASEEI
REKLQQVMSR RKEMNEKWEA RRERLHMLLE VCQFSRDASV AEAWLIAQEP YLASRDFGHT
VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTASRGGRR DSRRGSPSSP CSHRENVPGQ
FPVPMV
//
