ID A0A340WAV7_LIPVE Unreviewed; 2411 AA.
AC A0A340WAV7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Spectrin alpha chain, erythrocytic 1-like {ECO:0000313|RefSeq:XP_007445646.1};
GN Name=SPTA1 {ECO:0000313|RefSeq:XP_007445646.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007445646.1};
RN [1] {ECO:0000313|RefSeq:XP_007445646.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_007445646.1; XM_007445584.1.
DR STRING; 118797.A0A340WAV7; -.
DR GeneID; 103089563; -.
DR KEGG; lve:103089563; -.
DR CTD; 6708; -.
DR InParanoid; A0A340WAV7; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000265300; Unplaced.
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:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 11.
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; 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:SF431; SPECTRIN ALPHA CHAIN, ERYTHROCYTIC 1; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR01887; SPECTRNALPHA.
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; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
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:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 968..1027
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2263..2298
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2306..2341
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 858..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1312..1374
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2184..2218
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2411 AA; 279651 MW; D46376AE72B54A1E CRC64;
MESGGPKVLE TAEEIQERRQ EVLTRYQRFK ELVAERGQKL EDSYYYQVFI RDADDLEKWI
LEKIKIAGDK SYEDPTNIQG KYQKHESFEA EVQAKSRVIP ELEETRKVRF PEGHFAHEDT
KVLLEELSHL WDLLLELTQE KGTLLLRALK LQQYLQECAD ILEWIGDKEV IVTSVELGED
WERTEVLHKK FEDFQADLAV RKERVNGVNQ YANECAEEKH PELPLIQSKQ EEVNAAWERL
HGLALQRQKM LSSASDLQRF KRDLTEAIQW IKEKEPQVTS EDYGKDLVSS EALFHSHKTL
ERNLAVMNDK VKELCAKADK LKLSHPSDAA QIQQMKEDLV SNWGHIRTLA TSRYEKLQAS
YRYQRFLSDY DELSGWMKEK TALINADELP TDVTGGEALL DRHQQHKHEI DSYDDRFQSA
NETGRALLDA SHEASDEVMD KMAVLTSHWD ALLELWDKRW QQYEQCLELH LFYRDSEQVD
SWMSRQEAFL ENEDLGNSLG SVEALLQKHD DFEEAFTAQE EKITTLDKTA TKLIDNDHYD
SENIAAIRDG LLARQNALRE RAATRRRLLE DSLLLQQLYQ DSDDLKNWIN KKKKLADDED
YKDTQNLKSQ VQKQQVFEEE LAANEIQLNN IQKTGQEMIE SNHYASESVD VRLSEVAKLW
TELLEATAQK GTQLYEANKQ LQFENNAEDL KHWLEEVEWQ ARSEDYGKGL SDIQNLLRKH
SLLESSMAAR QDQVDTLTDL AAYIEEIGHP NAGDIRARQE SLVSRFEDLK KQLANRKNKL
IDLLLLHQIC RDTEDEEAWI QETEPSAAST YLGKDLIASK NLLSRHQVIQ ANIASHEPRI
KVITERGNKM IEEGHFAAED VASRVKSLNE NMESLQARAA RRQNDLEANV QFQQYLADLH
EAEAWIREKE PIVDNTNYGA DEEAAGALLK KHEAFLVDLK AFGNSMQALR DQAEACQQQQ
AAPMEEAARE ERVVALYDFQ ARSPREVTMK KDDILTLLSS INKDWWKVEA DDHQGFVPAV
YVRKLARDEF PMLPQRRREE PGNITQRQEQ IENQYLSLLD RAEERRRHLL QRYNEFLLAY
EAGDMLDWIR EKKAENSGVE LDDVWELQKK FDEFQMDLKT NEPRLRDINK VADDLQFEEL
LTPEGAQIQQ ELNARWGSLQ RLAEEQRQML GSAHAVQMFH READDTKEQI EKKCQALSAA
DPGSDLFSVQ ALQRQHEGFE RDLIPLEEKV AVLGETADRL SESHPDATDD LQRQRLELNQ
AWDDLLGLTE ERKENLQEDL KFFLFLSQAR DQQNWLSGIG SMISSQELAE DLTGTEIMIE
RHQEHLAEME AEAPTFQALE DFGTDLISSG HRASPKIEET LQAVKLERDE LEKAWEQRKK
MLDQCLELQF FRGNCDQAES WMVVRENYLR SDDKGSLDSL EALMKKRDDL DKAITAQEKK
ITELELFAEQ LIADDHYAQE EIAARRQRVL DRWKALKEQL IAERTKLGDY ADLKQFYHDL
KDQEEWISEM LPIACDESYK DPTNIQRKYL KHKTFENEVY GRAEQVKGVI TLGNTLIKRR
ACDGNEETMK GQVEELEKNW DYLLERTIDK GQKLNEASRQ QRFNTAIRDF EFWLSEAETL
LSMKDHARDL ASAGNLLKKH QLLETEMLAR KDALKDLNTL AADLISSGTF NTDQIVEKRD
NVNERFLNVQ KLAAEHHEKL KEAYALFQFF QDLDNEEFWI EEKLVRVRSQ DYGRDLQGVQ
NLLKKHKRLE GELVAHEPII QNVLDMAERL GDKAAVGREE IRERLDQFVQ HWDQLKELTK
ARGIQLGESL EYLEFMENAE EEEAWISEKE AMVTQGDSGD TLAATQSLLK KLEALENDFA
VHEIRVQNVC AQGEDILSKV LQEESQHKEK ISTKIEALKE KTPSLAKAMA AWKLQLEDDY
DFQQFNWKAD VVEAWIAEKE TSLKTNGNGA DLAAFLTLLA KQDTLHASLQ SFQQERLSEI
TDLKDQLVAA EHSQTGAIKE RHAALLRLWE QLLEASEAHR QELLEKQLPL LKAEDLFMKF
AHKASAFNNW CENAEEDLSE PVRCVSLDAI QRLKKDHEDF LASLARAQGD FNYLLELDQQ
IKALNVSSSP YTWLTVEVLE RIWNHLSDIV KEREQELEKE EARQVKNFEM CQEFEQNASA
FLDWIVQTRD YFLDGSLLKE TGTLESQLEA NKRKQKEIQA MKRKLTKIED LGENLEEALV
LDIKYSTIGL AQQWDQLYQL GMRRQHSLEQ QIQARDITGL SEETLQEFQT AFRHFDENLT
GRLSHKDFRS CLRGLNYYLP MVEEGEPEPK FEKFLDAVDP GRKGYISQTD YTDFLIDKES
ENIKSSNELE DAFQALAEGK AYITKEDMKQ ALTPEQVSFC ASHMQQYMDP RGRSQPAGYD
YVGFISSYFG K
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