ID A0A087Y0P3_POEFO Unreviewed; 2376 AA.
AC A0A087Y0P3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN2 {ECO:0000313|Ensembl:ENSPFOP00000011596.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011596.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011596.2}
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 EMBL; AYCK01009660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000011596; -.
DR Ensembl; ENSPFOT00000011612.2; ENSPFOP00000011596.2; ENSPFOG00000010957.2.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000158847; -.
DR OMA; DNHEPWI; -.
DR Proteomes; UP000028760; 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; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd21317; CH_SPTBN2_rpt1; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.20.58.60; -; 12.
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; 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:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 58..162
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 177..282
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2214..2324
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2088..2136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2323..2376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 995..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1101..1128
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1240..1278
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1426..1453
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1849..1883
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2088..2105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2178..2202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2355..2369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2376 AA; 272413 MW; 3B61DCE385BAD1EF CRC64;
TMSTISPTDF DSLEIQQQYN DINNRWDLAA ETDWDNENSS ARLFERSRIK ALADEREAVQ
KKTFTKWVNS HLGRVTCRIG DLYTDLRDGR MLIRLLEVLS GEQLPKPTKG RMRIHCLENV
DKALQFLKEQ KVHLENMGSH DIVDGNHRLT LGLIWTIILR FQIQDISVET EDNKEKKSAK
DALLLWCQMK TAGYPNVNIH NFTTSWRDGL AFNAIVHKHR PDLIEFDNLK RSNAHYNLQN
AFNVAEKEMG LTKLLDPEDV NVDQPDEKSI ITYVATYYHY FSKMKALAFK TKNFLSVLDY
AIEADQLIEK YETLASELLQ WIEQTILTLN DRQLANSLSA VQNQLQAFNS YRTVEKPPKF
TEKGNLEVLL FTIQSKMRAN NQKVYMPKEG KLISDINKAW ERLEKAEHER ELALRNELIR
QEKLEMLAAR FDRKAAMRET WLSENQRLVS QDNFGTDLGA VEAATRKHEA IETDIGAYWE
RVAAVEAVAK ELEAEKYHDV RRILARRDNV LRLWEYLKEL LAARRERLNS HRDLQRLFQE
MRYIMDWMAD EKGRLQSQDS GKHLHDVLDL LQKHNLVEAD ISGQAERIKA VQGAAKRFTS
YDQAYKPCEP GLVSEKVDLL GQAYEELGQL AATRRERLED SRRLWQFMWD LGEEAAWIRE
QEQILASGDS GRDLSSALHL LSKHEAFRDE MAARYGPLSN SIAAGEALVE EGHFGAPEIT
ERIQDVRGQW AHLEETTKLR EQSLKESVAL HQFQTDANDM EAWIMETLRQ VSSQEVGHDE
FSTQTLARKQ REIEEEIQSH RPLIDSLHEQ AQALPEAYIH FPEVEGRLPA IEQRYEELES
LSAARRQALE GALALYRMFS EADACQLWVE EKEQWLDGME IPTKLEDLEV VQQRFDTLEP
EMNNLGARVT DVNQVAEQLL SSDNCSKDQI HQTRDQLNDR WKEFEKLAGQ KKQALESALN
IQNYHLECNE SQTWMKEKTK VIESTQSLGN DLAGVMALQR KLTGMERDLE AIQGKLDDLT
KEAEKLASEH PDQAGEIQGR LAEIQEVWEE LNATMKRREE SLGEASKLQG FLRDLDDFQS
WLSRTQTAVA SEDIPTSLPE AESLLAQHES IKNEVDNYKE DYEKMRAVGE EVTQGQTDAQ
HMFLAQRLQA LDTGWHELRR MWENRHSLLA QAFDFQTFLR DAKQAEAFLN SQEYVLSHTE
MPTNLQAAEE AIKKHEDFLT TTEASEEKIT GVVEAGRRLI NDSNANADKI QEKVDSIQER
HCKNKEAANE LLAKLKDNCE LQRFLQDGQE LTLWINEKML TAQDMTYDEA RNLHSKWQKH
QAFMAELASN KDWLDKIDKE GQALVAEKPE LKPVVQQTLE DLQRQWEELE STTRTKDQCL
FEAHRAEIFT QSCSALDDWL KNIETQLHSD DYGKDLTSVN ILLKKHQMLE HQMEVREKEV
QSLQSQAVAL SQEDAGLAEV DGQQKRVIDS FSSLQDPLNL RRQQLLASKE AHQFNRDLED
EILWVKERMP LATSIDHGKD LPTVQLLIKK NQTLQKEIQG HQPRIDDIHR RGEAQSQVDG
DRQSLLKERL VELRDLWDQL IAETDKRHDR LIEANRAQQF YADAAEAEAW MGEQELHMMS
EEKAKDEQSA LAMVKKHQVL EQALEDYAQT IHQLANSSRL MVTSEHPESE RITLRQAQVD
KLYAGLKDLA EERRGRLQER LRLTQLKREV DDLEQWIAER EVVAGSHELG QDYEHVTMLR
DKFREFARDT STIGQERVDG VNALADDLIE SGHPENASVA EWKDGLNEAW ADLLELIDTR
TQMLAASYEL HRFHQDAMEV LGRIKEKKEA VPSDLGRDLN TVQHLHRQHN TFENDIQALS
GQVNQVQDDA ARLQKAYAGE KADDIQKSET AVTTAWQGLL EAGKARRLLL LDTVEKFRFL
NMVRDLMLWM DGINVQIDAH ESPRDVSSAE LVIINHKGIK SEIETRADSF TASTKMGNDL
INKNHYASDE IREKMAQLQE KRDEINSKWQ EKMDHLQIVL EVLQFGRDAN VAESWLAGQE
PLVRAAELGA NVDEVESLIK RHEAFEKLAA AWEERFVQLE KLTTLEEHEM QRRREEEERA
RRPPTPPPVE EVVPSEPDSQ PHDSAARHRT SLDQTTLNQS VAVNGVHSDN DTSQSLLEQH
AHFIFYSGGG EGPGEKTGSE SDSVNGPGRD SGLASSRLEP SATLPSRGGA DSEPETMEGI
LCRKQEMESH NKKAATRSWQ NVYCVLRKGS LGFYKDSKSA SNGIPYHGEV PIGLDGSVCE
VAHDYKKRKH VFKLRLGDGK EYLFQAKDEA EMSSWIQSIA GSIPSGAGDS PGAPRLSRAM
TMPPISPSSG EGVTMRNKEG KEKDREKRFS FFGKKK
//
