ID F7AN80_XENTR Unreviewed; 2545 AA.
AC F7AN80;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=sptbn4 {ECO:0000313|Ensembl:ENSXETP00000036874,
GN ECO:0000313|RefSeq:XP_002938861.2,
GN ECO:0000313|Xenbase:XB-GENE-1013360};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000036874};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000036874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000036874};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000036874}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002938861.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002938861.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002938861.2};
RG RefSeq;
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 RefSeq; XP_002938861.2; XM_002938815.5.
DR Ensembl; ENSXETT00000036874; ENSXETP00000036874; ENSXETG00000002566.
DR GeneID; 100488521; -.
DR KEGG; xtr:100488521; -.
DR AGR; Xenbase:XB-GENE-1013360; -.
DR CTD; 57731; -.
DR Xenbase; XB-GENE-1013360; sptbn4.
DR eggNOG; KOG0517; Eukaryota.
DR HOGENOM; CLU_000146_1_0_1; -.
DR OMA; LTSCEDC; -.
DR TreeFam; TF313446; -.
DR Reactome; R-XTR-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-XTR-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-XTR-5673001; RAF/MAP kinase cascade.
DR Reactome; R-XTR-6807878; COPI-mediated anterograde transport.
DR Proteomes; UP000008143; Chromosome 8.
DR Bgee; ENSXETG00000002566; Expressed in brain and 13 other cell types or tissues.
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; cd21318; CH_SPTBN4_rpt1; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 8.
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:SF232; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 4; 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; 16.
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; 16.
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:UP000008143};
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 DOMAIN 2397..2507
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2209..2398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2522..2545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..739
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1097..1131
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1415..1442
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1633..1660
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1846..1873
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2144..2184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2212..2304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2318..2332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2528..2545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2545 AA; 294396 MW; 9346D52C432AB87C CRC64;
MANVSPELDN MEVQTPPNNN NRWEQKEHPW DEPAATGKLF ECSRIKALAD ERDAVQKKTF
TKWINSHLSK VPLRVNDLYT DLRDGYIITK LLEVLSGEQL PKPTRGRMRI HYLENVDKAL
QFLKEQRVHL ENVGSHDIVD GNHRLTLGLI WTIILRFQIQ VIRIETEDSR ETRSAKDALL
LWCQMKTSGY PEVNIQNFTT SWRDGLAFSA LIHRHRPDVI DFNKLTKSNA TYNLQHAFNT
AEQQLGLTKL LDPEDVNMEH PDEKSIITYV VSFYHYFSKM KALAVEGKRI GKVLDKAIET
EKDIVKYEVL ASELLEWIER TIAIITNQKF ANSLLGVQQQ LQVFTTYCTT EKPCKFQEKG
NLEVLLFSIQ SKMREEKCKL YVPSEGKNIS DINKAWACLE KAEHEREVAL RNELIRQEKL
ELLSQRFDQK AAMREAWLSE NQRLVSQDNF GYDLPAVEAA MKKHEAIEAD ISSYEERIQV
VADLAQELEA EGYYDICRIS AQKDNILRQW NLLKDMLSSR RARLEQNLSL QKIFQEMVYM
IDWMDEMQVP LSSKDFGKHL LEVEDLLQKH CLLEADIAAQ TERVNSLNQA ALKFTQMTDY
QPCDPQVICN RVEHVRSCLE GLRQLAEKRR GELEESRRLW CFLQEVEEAE GWIREKEQIL
SAPQSYGKDL SSVLRLLSKH KILVGELRGR HAMLQQTLQK GEQVLAKRRK GMSGLRQRME
QVRLKWENLQ KACDNHQQKL QEASSFYQFS ADTMELAGWL QDTYRLVSSD DFGHDEYSTQ
SLVKKHRAET VEIEKHKVAV LGLRQQLSEL GAEYRDQVDV QITIVEVEQL YGEVVEVSAL
RSQWLQDALD VYKMFGEVNS CEVWIDEKEQ WLMKMEIPQR LEEVEVVQHR FESLDQEMNS
LMGRVLDVNQ IVQQLLEGGH PSSSEVRACQ DHLNSRWNRI VELVEQRKEQ LSSVLRLQNY
FLECNEVKSQ IREKRRTMET PQCGSGELGG VLSLQRKLSS MEAALLALEP KLVQLQQDAE
ILATSHPSQA MEVLVHFEEI SGEWDALKRT LQGCEDSLTV ANKLQQFIQD LDNFLTWLVK
TQTAVAAEEL PSNLAEAERL LGLHGSLKEE ISRYEEEYNK IQAVNDLLSL EEADLPYLSL
QQWLQKLEVG WNKLLQMWEN RREVLVQAHI FHLFLRDFKQ AEACLNTQES TLAHVELPNT
VEGVEAAIKK HKDFVTTMEL NVQKVSVAVE AGESLIRLGN VFADHVQERI SAIQKRSQRN
TALAQKWLQR LRDHLQLQHF LQNCNELDAW VHEKTLMARD SSRDLSQKPH KKWLKHQAFM
AELSQNKGWL EKIEKEGQQL IQEKPELAGV VKKKLEEIRQ CWVELESSTQ AKAQQLFQAT
KADQVVQNYS ELGKRLYHLK EQLQPVDPVP DVSSVNTQLK RLETMESQME EWYKEVGELQ
AQIASLPLEV ASQKALEEKQ NEVGTTIVRL IEPLKERRRI LLASKEVHQV TRDLEDEIFW
VQERLPLATS KEHGSNLQIV QQLIKKNQNL RREIQVHSPR VDDILERAGA IASIRTPEAE
GVRLGYESLG EMWNMLRDET ERRQQLLDIT YQVQQYYFDV GEVETWLSEQ ELLMMNDEKG
KDEQSTLQLL KKHLMLEQTI ENYEETIAQL SRQCRTLLDL GHPDSEQISK RQSQIDRLYV
SLKDLVDERK GRLEQQYWLF QLSREVDELE QWIAEKEVVA GSPELGQDYE HVTLLQEKFT
EFATETGSVG QERISAVNQM VDELIDFGHS DAAIIAEWKD GVNEAWADLL ELMETRSQML
AASHELYKFF NDCKEVLSQV EEKKQRLPEV KAQEAKLSAG SLQRILSSFE HDIQVLVTQV
RQLQENAAQL RTVYAGENAA AIVTSEQEVM RAWKELLTSC EDCRLQITST TDRIKFLNLV
RDLISWMESI TCQIGAEEKP RDVSSVEVLM SYHQGLKSEI ESRNKRIADC VELGKTLVLN
KRPSSDEIKQ SLDRLMAKKK EMLEKWNKHW EWLQQMLEVH QFAQEAGVAD AWLTAQEPIV
KSPELGNSVD EVEQLIRRHE AFRKTAAVWE ERFSSLRRLT TLEKLKAEQS KQPATPLLGR
KVFPDTTDYS ARPSPLSRQT VYENSETKLD QKEALSIPDG GQQEIRRARA EKGETRVGYV
RQDIKPERLQ PKMDHVETKV ADKPLAAQEV ERAEKTEIKF AQGMANLTVE KPEIKGSRHT
ERKRDRHERR LERQESSEQE TPKQEPPERR RDRHEKRLER QGSSEQETPK QEQSERRRDR
HERRTERQDT IEQDKPRTEP EKQAGKATLA DIVEQLQEKE AFQNSSGGQD SPARVPNGVD
KLPERTTRPD RPRARDRPKP RRRPRPKDPN QPPGEARRSR SAPAQSSAPP PPPPTHTIQQ
EGYLFRKHEL DGPSKKASNR SWINLYCVLN KGDLGVYKDA KSQSSGATHG GEPLLNLLGA
SCEVASEYKK KKFVFKLRST DGREFLFQAK DEEEMKNWIT AITTCVSQHA EIARWSQSLL
TTSSTDEGNI KRETERRPSG GGRKK
//
