ID A0A3P9NK20_POERE Unreviewed; 2545 AA.
AC A0A3P9NK20;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Spectrin alpha, non-erythrocytic 1 {ECO:0000313|Ensembl:ENSPREP00000009897.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009897.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009897.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009897.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826}.
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DR Ensembl; ENSPRET00000010013.1; ENSPREP00000009897.1; ENSPREG00000006662.1.
DR GeneTree; ENSGT00940000156662; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006662; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 13.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.60; -; 19.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00054; EFh; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 16.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1033..1092
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2396..2431
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2439..2474
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1226..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 250..284
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 356..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 452..482
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1191..1225
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1766..1800
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2017..2044
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2245..2277
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1233..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2545 AA; 291976 MW; 64503BB684DAD6AB CRC64;
MFVLLENEVT PSPARIRVLP SNFGCFRTAA GVTSCHRAPR PSDEPSGSIL RDNVFSTSSL
GKNLTKMDTV GVKVLETAED IQERRQQVLD RYRRFKELSM VRRQKLEDSY RFQFFRRDAD
ELEKWIQEKL QIASDENYKD PSNLQGKLQK HQAFEAEVQA NAAAIIELDK TGNLMTTEGH
FASETIRSRL EELHRLWDLL LQKTKEKGMR LLQAQKLVQY LRECEDALDW ISDKEAIVTS
EELGQDLEHV ELLQKKFEEF QTDLAAHEER VNEVNQLAGK LIQEAHPENE LIVRKQEEVN
AAWQRLKGLA LQRQTRLFGS AEVQRFNRDV DETISWIKEK EQLMASDDFG RDLASVQALL
RKQEGLERDL AALKDKVNTL GGDAERLQQT HPQNASQIHL KKDELITNWE QIQTLAAERH
ARLNDSYHLQ RFTADFRDLT SWVTEMKALI NADELANDVA GAEALLDRHQ EHKGEIDAHE
DSFRTTDEAG QALLSAGHYA SEEVKEKLGI LAQEKESLLE LWEVRRQQYE QCMDLQLFYR
DTEQVDNWMS KQEAFLLNED LGDSLDSVEA LLKKHEDFEK SLSAQEEKIT ALDEFATKLI
QNSHYAKEDV ATRRDALLSR RNALHERAQA RRAALEDSFH LQQFFRDSDE LKSWINEKMK
TATDESYKDP SNLQGKVQKH QAFEAELSAN QSRIDALQKS GQELLDRKHY ASAEVTARME
DVSAQWKKLL EATELKGIKL REANQQQQFN RNVEDIELWL YEVEGHLASD DYGKDLTSVQ
NLQKKHALLE ADVAAHQDRI DGITIQARQF QEAGHFDADN IQKKQEALVV RYEALREPMA
ARKQKLSDSL RLQQLFRDVE DEETWIREKE PIASSTNRGK DLIGVQNLLK KHQALQAEIT
GHEPRIKAVT QKGETMVEEG HFAGEEVKAK LGELHGRWDT LKGKAGQRRQ DLEDSLQAQQ
YFADANEAES WMREKEPIVG SPDYGKDEDS AEALLKKHEA LMSDLTAYGS SIQALKEQAQ
SCRQQVAPTD DETGKELVLA LYDYQEKSPR EVTMKKGDIL TLLNSTNKDW WKVEVNDRQG
FVPAAYVKKL DPTQSSSREN LLDEHGSIAA RQEQIDNQLV TKEPCSVSVR MKQVEELYGT
LLELGEKRKD MLEKSCKKFM LFREANELQQ WIHEKESALT NEEVGSDLEQ VEVLQKKFDD
FQKDLKANES RLRDINKVAS ELESEGLMAE EAPTVQAQQQ EQLGSAPGKD ESDSKTASPW
KTIRLGVQTT ANFNTIKELN NRWRSLQQLA EDRSNMLGSA HEVQRFHRDA DETKEWIEEK
NQALNTDNYG HDLASVQALQ RKHEGFERDL AALGDKVKSL GETAERLIQS HPEAVDDIQE
KCTELNTAWS SLVGRADQRK EKLGNSHDLQ RFLSDFRDLM SWINGIRGLV SSEELAKDVT
GAEALLERHQ EHRTEIDARA GTFQAFEQFG QQLLARGHYA SADVQQKLKA LDQERADLEK
AWVQRRMMLD QCLELQLFNR DCEQAENWMA AREAFLASDD KGDSLDSVEA LIKKHEDFDK
AINVQEEKIA ALQSFADQLI GADHYAKPEI YNRRNEVLDR WRRLKAQMIE KRSKLGESQT
LQQFSRDVDE IEAWISEKLQ TATDESYKDP TNIQLSKLLS KHQKHQAFEA ELHANADRIK
GVIDTGNALI QRGACAGSED AVKARLSALD EQWQFLVNKS AEKSQKLKEA NKQQNFNTGI
KDFDFWLSEV EALLASEDYG KDLASVNNLL KKHQLLEADI SAHEDRLKDL NGQADSLMAS
NAFDTSQVKD KRDAVNGRFA KIKSMAAGRR AKLNESHRLH QFFRDLDDEE SWIKEKKLLV
GSEDYGRDLT GVQNLRKKHK RLEAELAAHE PAIQSVLDTG KKLSDDNTIG QEEIQQRLAQ
FVDHWKELKD LSGARGKRLE ESLEYQQFVA NVEEEEAWIN EKLNLVGGED YGDTLAAVQG
LLKKHEAFET DFTVHRDRVS DVCANGEELI KKNNHHVDNI SAKMAALRGK VSELERAAAQ
RKAKLDENSA FLQFNWKADV VESWIGEKEN SLKTDDYGRD LSSVQTLLTK QETFDAGLQA
FQQEGITNIT ALKDQLLAAK HVQSKAIEAR HAALIKRWNQ LLSNSAARKK KLLEAQEHFR
KVEDLFLTFA KKASAFNSWF ENAEEDLTDP VRCNSLEEIR ALREAHEAFR SSLSSAQTDF
SQLAELDQQI KSYQVVSNPY TWFTMEALEE TWRNLQKIIK ERELELQKEQ RRQEENDKLR
QEFAQHANAF HQWLQETRTY LLDGSCMVEE SGTLESQLEA TKRKHQEIRA MRSQLKKIED
LGAAMEEALI LDNKYTEHST VGLAQQWDQL DQLGMRMQHN LEQQIQARNT TGVTEEALKE
FSMMFKHFDK EKSGRLNHQE FKSCLRSLGY DLPMVEEGEP DPEFEAILDT VDPNRDGNVS
LQEYMAFMIS RETENVKSSE EIESAFRALS AENKPYVTKE ELYQNLTKEQ ADYCLSHMKP
YLDSKGRELP SAFDFVEFTR SLFVN
//
