ID G1LCQ9_AILME Unreviewed; 2363 AA.
AC G1LCQ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSAMEP00000004689.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000004689.1, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000004689.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000004689.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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_002914092.1; XM_002914046.3.
DR STRING; 9646.ENSAMEP00000004689; -.
DR Ensembl; ENSAMET00000004879.2; ENSAMEP00000004689.1; ENSAMEG00000004191.2.
DR GeneID; 100477448; -.
DR KEGG; aml:100477448; -.
DR CTD; 6711; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000154864; -.
DR HOGENOM; CLU_000146_1_2_1; -.
DR InParanoid; G1LCQ9; -.
DR OMA; EMPSAQM; -.
DR OrthoDB; 2872403at2759; -.
DR TreeFam; TF313446; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0032437; C:cuticular plate; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031430; C:M band; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR GO; GO:0021556; P:central nervous system formation; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0071709; P:membrane assembly; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; IEA:Ensembl.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IEA:Ensembl.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd21316; CH_SPTBN1_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:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 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; 15.
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|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR002297};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
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 2196..2306
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2088..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..491
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 990..1031
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1096..1123
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1421..1455
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1852..1879
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2088..2104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2105..2177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2340..2356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2363 AA; 274344 MW; C1ADC64FB60F1846 CRC64;
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIGIQ AERVRGVNAS AQKFATDGEG
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
LSSDDYGKDL TSVVRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERIL
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDVLRIASSN DVGHDEYSTQ
SLVKKHKDVA EEIANYRPTI DSLHEQAGAL PQEHAESPDV RGRLSGIEER YKEVAELTRL
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
QASRVAVVNQ IARQLMHSGH PSEKIKAQQD KLNTRWSQFR ELVDRKKDAL LSALSIQNYH
LECNETKSWI REKTKVIEST QDLGNDLAGV MALQRKLTGM ERDLVAIEAK LSDLQKEAEK
LESEHPDQAQ AILSRLAEIS DVWEEMKTTL KNREASLGEA SKLQQFLRDL DDFQSWLSRT
QTAIASEDMP NTLTEAEKLL TQHENIKNEI DNYEEDYQKM RDMGEMVTQG QTDAQYMFLR
QRLQALDTGW NELHKMWENR QNLLSQSHAY QQFLRDTKQA EAFLNNQEYV LAHTEMPTTL
EGAEAAIKKQ EDFMTTMDAN EEKINAVVET GRRLVSDGNI NSDRIQEKVD SIDDRHRKNR
EAASELLMRL KDNRDLQKFL QDCQELSLWI NEKMLTAQDM SYDEARNLHS KWLKHQAFMA
ELASNKEWLD KIEKEGMQLI SEKPETEAVV KEKLTGLHNM WEVLESTTQT KAQRLFDANK
AELFTQSCAD LDKWLHGLES QIQSDDYGKD LTSVNILLKK QQMLENQMEV RKKEIEELQS
QAQALSQEGK STDEVDSKRL TVQTKFMELL EPLNERKHNL LASKEIHQFN RDVEDEILWV
GERMPLATST DHGHNLQTVQ LLIKKNQTLQ KEIQGHQPRI DDIFERSQSI VTDSSSLNAE
AIRRRLADLK ELWGLLIEET EKRHRRLEEA HRAQQYYFDA AEAEAWMSEQ ELYMMSEEKA
KDEQSAVSML KKHQILEQAV EDYAETVHQL SKTSRALVAD SHPESERISM RQSKVDKLYA
GLKDLAEERR GKLDERHRLF QLNREVDDLE QWIAEREVVA GSHELGQDYE HVTMLQERFR
EFARDTGNIG QERVDTVNHM ADELINSGHS DAATIAEWKD GLNEAWADLL ELIDTRTQIL
AASYELHKFY HDAKEIFGRI QDKHKKLPEE LGRDQNTVET LQRMHTTFEH DIQALGTQVR
QLQEDAARLQ AAYAGDKADD IQKRENEVLE AWKALLDACE GRRVRLVDTG DKFRFFSMVR
DLMLWMEDVI RQIEAQEKPR DVSSVELLMN NHQGIKAEID ARNDSFTTCI ELGKSLLARK
HYASEEIKEK LLQLTEKRKE MIDKWEDRWE WLRLILEVHQ FSRDASVAEA WLLGQEPYLS
SREIGQSVDE VEKLIKRHEA FEKSAATWDE RFSALERLTT LELLEVRRQQ EEEERKRRPP
SPEPSTKASE ETESQQQWDT SKGEQVSQNG LPAEQGSPRM AETVDTSEMV NGAAEQRTSS
KESSPIPSPT SDRKAKTALP AQSAATLPAR TQETPSAQME GFLNRKHEWE AHNKKASSRS
WHNVYCVINN QEMGFYKDAK TAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLND
GNEYLFQAKD DEEMNTWIQA ISSAISSDKH EVSASTQSTP ASSRAQTLPT SVVTITSESS
PGKREKDKEK DKEKRFSIFG KKK
//