ID A0A674G8K2_TAEGU Unreviewed; 2445 AA. AC A0A674G8K2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 13-SEP-2023, entry version 15. DE SubName: Full=Spectrin alpha, non-erythrocytic 1 {ECO:0000313|Ensembl:ENSTGUP00000018874.1}; GN Name=SPTAN1 {ECO:0000313|Ensembl:ENSTGUP00000018874.1}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae; OC Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000018874.1, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000018874.1, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E., RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P., RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O., RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L., RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C., RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K., RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A., RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000018874.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSTGUT00000043953.1; ENSTGUP00000018874.1; ENSTGUG00000003937.2. DR GeneTree; ENSGT00940000156662; -. DR Proteomes; UP000007754; Chromosome 17. 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; 12. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.58.60; -; 20. 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:SF422; SPECTRIN ALPHA CHAIN; 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; 18. DR PROSITE; PS00018; EF_HAND_1; 2. 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:UP000007754}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 967..1026 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 2296..2331 FT /note="EF-hand" FT /evidence="ECO:0000259|PROSITE:PS50222" FT DOMAIN 2339..2374 FT /note="EF-hand" FT /evidence="ECO:0000259|PROSITE:PS50222" FT COILED 290..324 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 386..416 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1106..1140 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1672..1706 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 2151..2183 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 2445 AA; 281712 MW; 9C7CE519D55B536A CRC64; MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ RDADELEKWI QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAII KLDETGNQMI NESHFASETI RTRLQELHRL WELLMEKMRE KGVKLLQAQK LVQYLRECED VLDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAGKLIQETH PEEELIKSKQ DEVNASWQRL KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL ERDLAALEDK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA DESGQALLSA GHYASDEVKE KLTILSDERS ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MDDVATRRDA LLSRRNALHE RAMYRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VKHYASDEVA ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQEAGHF DADNIKKKQE ALVARYEALK DPMVARKQKL ADSLRLQQLF RDIEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID NQYHSLLELG EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAKDLESE GLMADEVQAV QQQEVYGMPR DETDSKTASP WKSARLMVHT VATFNSIKEL NERWRSLQQL AEERSQLLGS AHEVQRFHRD ADETKEWIEE KNQALNTDNY GHDLASVQAL QRKHEGFERD LAALGDKVNS LGETAQRLIQ SHPESAEDLQ EKCTELNQAW NSLGKRADQR KEKLGDSHDL QRFLSDFRDL MSWINGIRGL VSSDELAKDV TGAEALLERH QEHRTEIDAR TGTFQAFEQF GQQLLAHGHY ASPEIKEKLD ILEQERTDLE KAWVQRRMML DQCLELQLFH RDCEQAENWM AAREAFLNTE DKGDSLDSVE ALIKKHEDFD KAINVQEEKI AVLQSFADQL IAADHYAKGV IANRRNEVLD RWLRLKAQMI EKRSKLGESQ TLQQFSRDVD EIEAWISEKL QTASDESYKD PTNIQSKHQK HQAFEAELHA NADRIRGVID MGNSLIERGA CAGSEDAVKA RLAALADQWQ FLVQKSAEKS QKLKEANKQQ NFNTGIKDFD FWLSEVEALL ASEDYGKDLA SVNNLLKKHQ LLEADISAHE DRLKDLNSQA DSLMTSSAFD TSQVKDKRET INGRFQRIKG MASARRAKLN ESHRLHQFFR DMDDEESWIK EKKLLVSSED YGRDLTGVQN LRKKHKRLEA ELAAHEPAIQ GVLDTGKKLS DDNTIGKEEI QQRLAQFVDH WKELKQLAAA RGQRLEESLE YQQFVANVEE EEAWINEKMT LVASEDYGDT LAAIQGLLKK HEAFETDFTV HKDRVNDVCA NGEDLIKKNN HHEANITAKM KGLRGKVSDL EKAAAQRKAK LDENSAFLQF NWKADVVESW IGEKENSLKT DDYGRDLSSV QTLLTKQETF DAGLQAFQQE GIANITALKD QLLAAKHIQS KAIEARHASL MKRWNQLLAN SAARKKKLLE AQEHFRKVED LFLTFAKKAS AFNSWFENAE EDLTDPVRCN SLEEIKALRE AHDAFRSSLS SAQADFNQLA ELDRQIKSFR VASNPYTWFT MEALEETWRN LQKIIKEREL ELQKEQRRQE ENDKLRQEFA QHANAFHQWI QETRSCMVEE SGTLESQLEA TKRKHQEIRA MRSQLKKIED LGAAMEEALI LDNKYTEHST VGLAQQWDQL DQLGMRMQHN LEQQIQARNT TGVTEEALKE FSMMFKHFDK DKSGRLNHQE FKSCLRSLGY DLPMVEEGEP DPEFESILDT VDPNRDGHVS LQEYMAFMIS RETENVKSSE EIESAFRALS SEGKPYVTKE ELYQNLTREQ ADYCISHMKP YMDGKGRELP SAYDYIEFTR SLFVN //