ID M0QZQ3_HUMAN Unreviewed; 2002 AA.
AC M0QZQ3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN4 {ECO:0000313|Ensembl:ENSP00000470693.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000470693.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000470693.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000470693.1}
RP IDENTIFICATION.
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 EMBL; AC020929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; M0QZQ3; -.
DR MassIVE; M0QZQ3; -.
DR MaxQB; M0QZQ3; -.
DR PeptideAtlas; M0QZQ3; -.
DR Antibodypedia; 48036; 195 antibodies from 22 providers.
DR Ensembl; ENST00000595535.5; ENSP00000470693.1; ENSG00000160460.17.
DR UCSC; uc002onx.4; human.
DR HGNC; HGNC:14896; SPTBN4.
DR VEuPathDB; HostDB:ENSG00000160460; -.
DR GeneTree; ENSGT00940000156343; -.
DR HOGENOM; CLU_000146_0_0_1; -.
DR ChiTaRS; SPTBN4; human.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000160460; Expressed in right hemisphere of cerebellum and 152 other cell types or tissues.
DR ExpressionAtlas; M0QZQ3; baseline and differential.
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:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR CDD; cd21322; CH_SPTBN4_rpt2; 1.
DR CDD; cd00176; SPEC; 7.
DR Gene3D; 1.20.58.60; -; 9.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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; PF00435; Spectrin; 12.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 14.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 11.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
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|PIRNR:PIRNR002297};
KW Proteomics identification {ECO:0007829|EPD:M0QZQ3,
KW ECO:0007829|MaxQB:M0QZQ3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 61..165
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 180..285
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 464..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1445..1472
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1663..1690
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2002 AA; 225490 MW; E3CADCABF3302C6F CRC64;
MAQVPGEVDN MEGLPAPNNN PAARWESPDR GWEREQPAAS TAAASLFECS RIKALADERE
AVQKKTFTKW VNSHLARVGC HIGDLYVDLR DGFVLTRLLE VLSGEQLPRP TRGRMRIHSL
ENVDKALQFL KEQRVHLENV GSHDIVDGNH RLTLGLVWTI ILRFQIQVIK IETEDNRETR
SAKDALLLWC QMKTAGYPEV NIQNFTTSWR DGLAFNALIH RHRPDLVDFS KLTKSNANYN
LQRAFRTAEQ HLGLARLLDP EDVNMEAPDE KSIITYVVSF YHYFSKMKAL AVEGKRIGKV
LDQVLEVGKI IERYEELAAE LLAWIHRTVG LISNQKFANS LSGVQQQLQA FTAYCTLEKP
VKFQEKGNLE VLLFSIQSKL RACNRRLFVP REGCGIWDID KAWGELEKAE HEREAALRAE
LIRQEKLELL AQRFDHKVAM RESWLNENQR LVSQDNFGYE LPAVEAAMKK HEAIEADIAA
YEERVQGVAE LAQALAAEGY YDIRRVAAQR DSVLRQWALL TGLVGARRTR LEQNLALQKV
FQEMVYMVDW MEEMQAQLLS RECGQHLVEA DDLLQKHGLL EGDIAAQSER VEALNAAALR
FSQLQGYQPC DPQVICNRVN HVHGCLAELQ EQAARRRAEL EASRSLWALL QELEEAESWA
RDKERLLEAA GGGGAAGAAG AAGTAGGAHD LSSTARLLAQ HKILQGELGG RRALLQQALR
CGEELVAAGG AVGPGADTVH LVGLAERAAS ARRRWQRLEE AAARRERRLQ EARALHQFGA
DLDGLLDWLR DAYRLAAAGD FGHDEASSRR LARQHRALTG EVEAHRGPVS GLRRQLATLG
GASGAGPLVV ALQVRVVEAE QLFAEVTEVA ALRRQWLRDA LAVYRMFGEV HACELWIGEK
EQWLLSMRVP DSLDDVEVVQ HRFESLDQEM NSLMGRVLDV NHTVQELVEG GHPSSDEVRS
CQDHLNSRWN RIVELVEQRK EEMSAVLLVE NHVLEVAEVR AQVREKRRAV ESAPRAGGAL
QWRLSGLEAA LQALEPRQAA LLEEAALLAE RFPAQAARLH QGAEELGAEW GALASAAQAC
GEAVAAAGRL QRFLHDLDAF LDWLVRAQEA AGGSEGPLPN SLEEADALLA RHAALKEEVD
QREEDYARIV AASEALLAAD GAELGPGLAL DEWLPHLELG WHKLLGLWEA RREALVQAHI
YQLFLRDLRQ ALVVLRNQEM ALSGAELPGT VESVEEALKQ HRDFLTTMEL SQQKMQVAVQ
AAEGLLRQGN IYGEQAQEAV TRLLEKNQEN QLRAQQWMQK LHDQLELQHF LRDCHELDGW
IHEKMLMARD GTREDNHKLH KRWLRHQAFM AELAQNKEWL EKIEREGQQL MQEKPELAAS
VRKKLGEIRQ CWAELESTTQ AKARQLFEAS KADQLVQSFA ELDKKLLHME SQLQDVDPGG
DLATVNSQLK KLQSMESQVE EWYREVGELQ AQTAALPLEP ASKELVGERQ NAVGERLVRL
LEPLQERRRL LLASKELHQV AHDLDDELAW VQERLPLAMQ TERGNGLQAV QQHIKKNQGL
RREIQAHGPR LEEVLERAGA LASLRSPEAE AVRRGLEQLQ SAWAGLREAA ERRQQVLDAA
FQVEQYYFDV AEVEAWLGEQ ELLMMSEDKG KDEQSTLQLL KKHLQLEQGV ENYEESIAQL
SRQCRALLEM GHPDSEQISR RQSQVDRLYV ALKELGEERR VALEQQYWLY QLSRQVSELE
HWIAEKEVVA GSPELGQDFE HVSVLQEKFS EFASETGMAG RERLAAVNQM VDELIECGHT
AAATMAEWKD GLNEAWAELL ELMGTRAQLL AASRELHKFF SDARELQGQI EEKRRRLPRL
TTPPEPRPSA SSMQRTLRAF EHDLQLLVSQ VRQLQEGAAQ LRTVYAGEHA EAIASREQEV
LQGWKELLSA CEDARLHVSS TADALRFHSQ VRDLLSWMDG IASQIGAADK PRCPSSLLGL
PASPWWPTPA TPSPLTAPFS ME
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