ID M4AN88_XIPMA Unreviewed; 2360 AA.
AC M4AN88;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000015933.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000015933.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000015933.1};
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 Ensembl; ENSXMAT00000015957.2; ENSXMAP00000015933.1; ENSXMAG00000015871.2.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000158908; -.
DR HOGENOM; CLU_000146_1_0_1; -.
DR Proteomes; UP000002852; 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; cd21246; CH_SPTB-like_rpt1; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 9.
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; 14.
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:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 58..162
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 179..284
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2201..2311
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1252..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2108..2127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2170..2193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2310..2360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 463..497
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 889..923
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1003..1030
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1402..1449
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1570..1597
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1255..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2108..2126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2324..2338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2360 AA; 273515 MW; 2274D125D4625A9B CRC64;
MTSTTTSTTD FDNVEITQQY SHINTRFNLS DEELDNDNSS ARLFERSRIK ALADEREAVQ
KKTFTKWVNS ILSRVGCRIS DLYLDLRDGR MLIKLLEVLS GERLPKPTKG RMRIHCLENV
DKALQFLKEQ RVHLENMGSH DIVDGNHRLI LGLIWTIILR FQIQDIIVET GQADQKETHS
AKDALLLWCQ MKTAGYPNVN ITNFTNSWKD GMAFNALIHK HRPDLVDYTK LKRSNPTHNL
QNAFNVAEQK LGVTKLLDPE DVFTENPDEK SIITYVVAFY HYFSKMKQLA VEGKRVGKVL
DQAIETERMI DKYETLASDL LTWIEQTIVV LNNRKLANSL TGVQQQLQAF NTYRTVEKPP
KFQEKGNLEV LLFTIQSRMR ANNQRVYTPK EGALVSDINR AWERLERAEH ERERVLRDEL
IRQEKLEQMA RRFDRKAAMR ETWLLENQRL VAQDNFGYDL PAVEAAKKKH DAIETDIAAY
KERVQALVNI SKELESERYH DAKRIDVRKD NILRLWDYLQ ELLRSRRGRL DMNLTLQRIF
QEMLYIISWM DEMKARLLSP DFGKHLLEVE DLLQKHALLE NDIALQAERV QSASAAALKF
ANGDSYKPCD PQVIRDRVQH LNLCYQELCT LAAQRRARLE QSRRFWNCLW EVAELESWIR
EKEQLFSSLD YGKDLTSVLV LQSKHSAFED ELGARRNNLQ QVLAEGDKMI QAKHFGSPKI
QECMDDIKRQ WQQLEDLAAF RKQNLRDTQT FFQFQGDADE LKAWLLDAKR QMSSNDVGHD
EYTTQRLLKN QNNLRNEAIK NGATIDALSK QASALPEELQ NTPDIQRRLK DIKDLYMELL
TLADLRQKKL DDTMALYTIF SETDACELWM STKETWLVDL EVPENLEDLE VVQNRLSALA
QEMVNVQSRV DDVNKAAKQL EESRHPRTKD IKECQTRLNK RWEAFKAMVE DKKRRVDSAV
SLHNYGLECD ETETWIKEKT RVIESTQDLG NDLAAVMTIQ RKLFGMERDL AAIEAKLTFL
NEEANQLAQD HPENAADILA RRAELDTAWD RLRKTLKDRE DSLGEVSKLQ TFLQDMDDFQ
SWLFKTQKAV ASEEMPTSLQ EAEELLSRHN AVREDINNHE EDYHRVRDTG AQVTQGQEDD
PQYQQLEQRL NGLDRGWYEL QKMWDSRRNF LDQGLGFQQF LRDGKAVEAI LNNQEYTLAH
IDKPDTLAGA EKALKKHEDF VSTMEANEDK IDGALQGGQR LVDSNNLYSP KVQEKMDSVQ
DRQSKNKRRA VDVSEKLRDN RDLQHFLQNT QDLTVWINEK MLTAQDTSYD EARNLHSKWL
KHQAFMAELA SNKDWLNKVD QEGEELMESK PEFEPIVKER LAQLHELWDK LESTTQEKDR
LLFDANRSEL FDQSLADMKK WLAELQQQLQ SGDEDVKDLT NANIQLKKHQ MTENQVRDRA
RELDELQEAV RKHGGAREDQ PELEAEQQAL QSEFQQLLTP LSQRRGKLEA AKAVHQFYRD
LADELLWIEE RMPLAMSQEH GNNLQTVQML LKKNQTLQRE IEGHQPRVGE VLERGRRMAA
AASAEDRPEA ERIGDQMQEL EEAWARLRDE MAKRRERLSG SNLAQQYYND ADEAEAWIGE
QELYMIADEK AKDEQSAMLM LKRHLILKQA VDDYAASIQK LSDRAQKTLA EDHPDGEEII
RRQGQVDKQY AGLKELAEDR RKKLNHTYHH FLLSREVEDL EHWIAEKDVV ASSQEMGQDL
DHVTLLRDKF REFSRDMGMI GQDRVDMVNQ TIDELIETGH SEAATLAEWK DGINESWADL
LELIDTRSQL LTASYDLLKY FDDGKELVTQ IHEKQKELPE DVGDDFSKAE SFHRMHAAFE
RDITALGKQV QQFQETALRL RAQYAGDKQD AIQAMEREVV EAWKGLLDAS DGRRAELVDT
AEKFRFFSMV RDLMAWMESI IQQIETQEKP RDVSSVELLQ KYHQGIRSEI ETRSAKFTDC
IDLGKSMLTR KHRDSAEIKE KLVQLMEKRQ EMMFKWDDRW DWLRLLLEVC QFARDASVAE
AWLIAQEPYV TSRDLGQSVD EVEKLLKRHE AFEKSTATWE ERFSALERLT TLELLEVRKQ
QQEIEQFIKD EQRSDKESRR EDTGFVEESS QLYTIEEQTL SGAMEPSSGQ LDGTAGDSTM
PMVSEMRESA SLELEPSVSV VTPREPERAA TVPLETQRSQ AVLQEGMLCR KHDVEGSGKK
ASNRSWNNLY CVLKPGQLSA YKDAKSFGHG LTFHGEDPLP LGNATWESLT NYKKKKNVAK
LRLADGSEYL FQCKDEEELQ RWSQAMEKAV QTLAAEEAPG PSGSKTHSLP TAPSSSAALP
EPGSAKKDKE KKFSRFAKKK
//
