ID A0A401SPQ6_CHIPU Unreviewed; 2377 AA.
AC A0A401SPQ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN ORFNames=chiPu_0010817 {ECO:0000313|EMBL:GCC32356.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC32356.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC32356.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC32356.1}.
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DR EMBL; BEZZ01000429; GCC32356.1; -; Genomic_DNA.
DR STRING; 137246.A0A401SPQ6; -.
DR OMA; VHEFPYL; -.
DR Proteomes; UP000287033; 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; cd21317; CH_SPTBN2_rpt1; 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: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; 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; 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:UP000287033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 55..159
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 174..279
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2221..2331
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2092..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2334..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..492
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1097..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1247..1274
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1415..1442
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1557..1591
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2092..2138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2170..2191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2377 AA; 276899 MW; C375BF1B72385656 CRC64;
MTSATDFDNV EIQQQYSHIN ARWELSDEGE LDNDNSSARL FERSRIKALS DEREVVQKKT
FTKWVNSHLA RVTCRITDLY TDLRDGRMLI KLLEILSGEH LPKPTKGRMR IHCLENVDKA
LQFLKEQKVH LENMGSHDIV DGSHRLTLGL IWTIILRFQI QDITVETHDN RETRSAKDAL
LLWCQMKTAG YPNVNIRNFT SSWKDGMAFN ALIHKHRPDL VDFNKLKQSN ATYNLQQAFN
IAEQQLGVTK LLDPEDVYTE NPDEKSIITY VVAFYHYFSK MKALAVEGKR IGKVLDNAIE
TQKMIDKYEQ LASDLLIWIE QTIIVLNSRK FANSLAGVQQ QLQAFNTYRT VEKPSKFQEK
GNLEVLLFSI QSRMRANNQK VYTPHEGKLI SDINRGWERL EKAEHERELA LRNELIRQEK
LEQLARRFDR KALMRETWLC ENQRLVSQDN FGYDLSAVEA AMKKHEAIEA DIAAYEERVQ
TLVDVSLELE AENYHDIKRI NARKDNIMRL WEYLLELLNA RRARLEMNLA LQKIFQEMLH
IIDWMDEMKV RLLSQDFGKH LMGVEDLLQK HTLVEADIAI QADRLKLVNA GALKFAEDEG
YTPCDPNVIK DRVNHLELCY EELCVLAAER KARLEQSRCL WRFFWEMAET EGWIREREQI
FSSQDYGKDI TSIVILQSKH KALEDELGGL STHLQQTIKE GRDMIAQKHF ASPEIKKRID
EVLAMWKDLE ELAAFRKQNL QDAQNFFQFQ VDADDVKIWL QDTYRIVSSD DVGHDEFSTQ
TLVKKHRDLT DEIMKSGIAI DALNKQLQSL PEEFRKLPEI KDRQWEIKEL YADLVALADL
RRQRLQDALA LYIMFSEADA CELWMNEKEK WLEGVEIPKK LDDLEVVEHR FETLVQEMNN
LGSRITEVNS TANHLVETGH PSTQEVKECQ DHVNLRWLQF QKLVDMKKND VQSALSLQNY
CLECDETKVW ICEKTKLIES TQSLEKDLPG VLAIQRKLCG IERDLAAIES RLPELQKEAH
RLADQHPHHA ADILKRLKEI NDVWDELKHT LQGREESLGE ASKLQKFLQD LDDFQLWLSK
SQKAIASEDE PNSLPEAETL LQQHNAIKNE IDRNLEEYQK IQENGKMITE GETDPQFQIL
KQRLEGVDTG WNELLQMWEN RKNLLSQSHG YQQFLRDSKQ ADSILRNQEY SLVHVEMPKT
LETAEDVIKK HEGFVTTMDA NREKIIGTIN EGEKLINEDN NFKVKVVDKI QAIKERYQEN
MKQAKEVAAH LKDNRDLQHF LQNCQELIFW INEKMLTAQD TSYDEARNLH TKWQKHQAFM
AELASNKEWL DKVEKEGKQL MEEKPEFKPQ ISEKLQELTD LWNVLDVTTE SKAKRLFDAN
RSELFAQTRD DLNKWLTEVE LQLHSDDFGK DLTSVNILLK KLQILENQVD MRKKEVEELL
SQTRILSPEG LMETDGKEQD IERRFLQLMG PLQERRQKLH LSKMTYQFYR DLEDEILWVQ
ERMSLATSTD HGHNLQTVHL LMKKNKTLQK EIQGHQPRID DVLERGEAMV VEQRPDSVAI
EEQLKELKEL WNKLQEEAEK RQKRLEGANE AQQYYMDAAE AEIWMSEQEL YMIADEKTKD
EAGATTMLKK HLILQQAILD YGNIIREMAD RAQKLLTEEH PEGEQIIRRQ GQVDKLYAGL
RDLANERKKK LEDICHLLQL NREVMDLEQW IAERDVAASS QELGQDYDQV TLLREKFREF
ARETGTIGQE RVDSVNLLID DLIDSGHSEA ADIAEWKDSL NEAWADLLEL IDTRTQLLTA
SFELHKYFYD GKELLSLIQE KHEELPEDLG RDANTAESFH RMHSAFERDI HSLGIQVQQF
QDDAGHLQTA YAGDKAAAIQ KQEQEVVEAW KALLDACDGR RTQLVDTAEK FRFFSMVRDL
MSWMESIIRQ VETEEKPRDV SSVELLMKYH QGIRAEIDAR NRNFTSCIDL GKTMLARNHH
ASEEIRDKLV QLTEKRKSMM DKWEERWCWL RLLLEVCQFA RDASVAEAWL ITQESYLNSR
DIGNSVDQVE KLIKKHEAFE KSTATWDERF SALERLTTLE LLEIRKKQEA FRQTREAQLQ
PESELDHDQI PPDTDQQPAD QTDVEKTQEE EWKMEGPKGA ELTPHVTDEP SLITTSEDLS
ALVNGTDSPE EKTLESEDKS EFEEKLRERA SKPPPLVLSE LEQEKPRVSS TLPILTPKEQ
PAQCEGYLAR KHELEGPNKK ASNRSWITLY CALKSGELYF YKDSKNFSAG VTYHGADPLN
LKGASCEVAA DYKKKKHVFK LRLNNGSEYL FHDKDEEELH NWIRNLNAAI AEQDKPQSTR
HGEVKAHTLP LPTVIAPETS PGKKDKEKRF SLFAKKK
//
