ID A0A3B3YUX9_9TELE Unreviewed; 2376 AA.
AC A0A3B3YUX9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000030978.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000030978.1}
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 STRING; 48701.ENSPMEP00000030978; -.
DR Ensembl; ENSPMET00000032916.1; ENSPMEP00000030978.1; ENSPMEG00000021667.1.
DR Proteomes; UP000261480; 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; cd21317; CH_SPTBN2_rpt1; 1.
DR CDD; cd21321; CH_SPTBN2_rpt2; 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: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; 2.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 90..194
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 209..314
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 2120..2214
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 1027..1061
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1133..1160
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1272..1310
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1458..1485
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1881..1915
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2120..2137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..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; 272566 MW; E37E5E69FA5AD022 CRC64;
MSTISPTDFD SLEIQQQYND INNRWDLAAE TDWDNENSSA RLFERSRIKA LAGMLLDRDP
CLSPAAFVNQ VQYSNILEGR FKQLQDEREA VQKKTFTKWV NSHLGRVTCR IGDLYTDLRD
GRMLIRLLEV LSGEQLPKPT KGRMRIHCLE NVDKALQFLK EQKVHLENMG SHDIVDGNHR
LTLGLIWTII LRFQIQDISV ETEDNKEKKS AKDALLLWCQ MKTAGYPNVN IHNFTTSWRD
GLAFNAIVHK HRPDLIEFDN LKRSNAHYNL QNAFNVAEKE MGLTKLLDPE DVNVDQPDEK
SIITYVATYY HYFSKMKALA VEGKRIGKVL DYAIEADQLI EKYETLASEL LQWIEQTILT
LNDRQLANSL SAVQNQLQAF NSYRTVEKPP KFTEKGNLEV LLFTIQSKMR ANNQKVYMPK
EGKLISDINK AWERLEKAEH ERELALRNEL IRQEKLEMLA ARFDRKAAMR ETWLSENQRL
VSQDNFGTDL GAVEAATRKH EAIETDIGAY WERVAAVEAV AKELEAEKYH DVRRILARRD
NVLRLWEYLK ELLAARRERL NSHRDLQRLF QEMRYIMDWM ADEKGRLQSQ DSGKHLHDVL
DLLQKHNLVE ADISGQAERI KAVQGAAKRF TSYDQAYKPC EPGLVSEKVD LLGQAYEELG
QLAATRRERL EDSRRLWQFM WDLGEEAAWI REQEQILASG DSGRDLSSAL HLLSKHEAFR
DEMAARYGPL SNSIAAGEAL VEEGHFGAPE ITERIQDVRG QWAHLEETTK LREQSLKESV
ALHQFQTDAN DMEAWIMETL RQVSSQEVGH DEFSTQTLAR KQREIEEEIQ SHRPLIDSLH
EQAQALPEAY IHFPEVEGRL PAIEQRYEEL ESLSAARRQA LEGALALYRM FSEADACQLW
VEEKEQWLDG MEIPTKLEDL EVVQQRFDTL EPEMNNLGIR VTDVNQVAEQ LLSSDNCSKD
QIHQTRDQLN DRWKEFEKLA GQKKQALESA LNIQNYHLEC NESQTWMKEK TKVIESTQSL
GNDLAGVMAL QRKLTGMERD LEAIQGKLDD LTKEAEKLAS EHPDQAGEIQ GRLAEIQEVW
EELNATMKRR EESLGEASKL QGFLRDLDDF QSWLSRTQTA VASEDIPTSL PEAESLLAQH
ESIKNEVDNY KEDYEKMRAV GEEVTQGQTD AQHMFLAQRL QALDTGWHEL RRMWENRHSL
LAQAFDFQTF LRDAKQAEAF LNSQEYVLSH TEMPTNLQAA EEAIKKHEDF LTTTEASEEK
ITGVVEAGRR LINDSNANAD KIQEKVDSIQ ERHCKNKEAA NELLAKLKDN CELQRFLQDG
QELTLWINEK MLTAQDMTYD EARNLHSKWQ KHQAFMAELA SNKDWLDKID KEGQALVAEK
PELKPVVQQT LEDLQRQWEE LESTTRTKDQ CLFEAHRAEI FTQSCSALDD WLKNIETQLH
SDDYGKDLTS VNILLKKHQM LEHQMEVREK EVQSLQSQAV ALSQEDAGLA EVDGQQKRVI
DSFSSLQDPL NLRRQQLLAS KEAHQFNRDL EDEILWVKER MPLATSTDHG KDLPTVQLLI
KKNQTLQKEI QGHQPRIDDI HRRGEAQSQV DGDRQSVLKE RLVELRDLWD QLIAETDKRH
DRLIEANRAQ QFYADAAEAE AWMGEQELHM MSEEKAKDEQ SALAMVKKHQ VLEQALEDYA
QTIHQLANSS RLMVTSEHPE SERITLRQAQ VDKLYAGLKD LAEERRGRLQ ERLRLTQLKR
EVDDLEQWIA EREVVAGSHE LGQDYEHVTM LRDKFREFAR DTSTIGQERV DGVNALADDL
IESGHPENAS VAEWKDGLNE AWADLLELID TRTQMLAASY ELHRFHQDAM EVLGRIKEKK
EAVPSDLGRD LNTVQHLHRQ HNTFENDIQA LSGQVNQVQD DAARLQKAYA GEKADDIQKS
ETAVTTAWQG LLEAGKARRL LLLDTVEKFR FLNMVRDLML WMDGINVQID AHESPRDVSS
AELVIVNHKG IKSEIETRAD SFTASTKMGN DLINKNHYAS DEIREKMAQL QEKRDEINSK
WQEKMDHLQI VLEVLQFGRD ANVAESWLAG QEPLVRAAEL GANVDEVESL IKRHEAFEKL
AAAWEERFVQ LEKLTTLEEH EMQRRQEEEE RARRPPTPPP VEEVVPSEPH SQTSLDQTTL
NQSVAVNGVH SDNDTSQGSE SDSVNGPGRD SGLASSRLEP SATLPSRGGA DSEPETMEGF
LYRKQEMESH NKKAATRSWQ NVYCVLRKGS LGFYKDSKSA SNGIPYHGEV PIGLDGSVCE
VAHDYKKRKH VFKLRLGDGK EYLFQAKDEA EMSSWIQSIA GSIPSGAGDS PGAPRLSRAM
TMPPISPSSG EGVTMRNKEG KEKDREKRFS FFGKKK
//
