ID A0A2U4B5N2_TURTR Unreviewed; 2217 AA.
AC A0A2U4B5N2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Spectrin alpha chain, erythrocytic 1 isoform X3 {ECO:0000313|RefSeq:XP_019788476.2};
GN Name=SPTA1 {ECO:0000313|RefSeq:XP_019788476.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019788476.2};
RN [1] {ECO:0000313|RefSeq:XP_019788476.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019788476.2};
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_019788476.2; XM_019932917.2.
DR Proteomes; UP000245320; Chromosome 1.
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; 10.
DR Gene3D; 1.20.58.60; -; 17.
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; 18.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 18.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 15.
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:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 768..827
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2069..2104
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2112..2147
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 658..689
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1112..1174
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1990..2024
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2217 AA; 256998 MW; DC41F65F2E4D4330 CRC64;
MLSHLSVDHA FFMCSKKEKH PELPLIQSKQ EEVNAAWERL HGLAVQRQKM LSSAADLQRF
KRDVTEAIQW IKEKEPQVTS EDYGKDLVSS EALFHSHKTL ERNLAVMNDK VKELCAKADK
LKLSHPSDAV QIQQMKEDLV SNWGHIRTLA TSRYEKLQAS YRYQRFLSDY DELSGWMKEK
TALINADELP TDVTGGEALL DRHQQHKHEI DSYDDRFQSA NETGQALLDA SHEASDEVMD
KMAVLTSHWD ALLELWDKRW QQYEQCLELH LFYRDSEQVD SWMSRQEAFL ENEDLGNSLG
SVEALLQKHD DFEEAFTAQE EKITTLDKTA TKLIDNDHYD SENIAAIRDE LLARQNALRE
RAATRRRLLE DSLLLQQLYQ DSDDLKNWIN KKKKLADDED YKDTQNLKSQ VQKQQVFEEE
LAANEIQLNN IQKTGQEMIE SNHYASESVD ARLSEVAKLW TELLEATAQK GTQLYEANKQ
LQFENNAEDL KHWLEEVEWQ ARSEDYGKGL ADIQNLLRKH GLLESAMAAR QDQVDTLTDL
AAYIEEIGHP NAGDVRARQE SLVSRFEDLK KQLANRKNKL IDLLLLHQIC RDTEDEEAWI
QETEPSAAST YLGKDLISSK NLLNRQQVIQ ANIASHEPRI QVITERGNKM VEEGHFAAED
VASRVKSLNE NMESLQARAA RRQNDLEANV QFQQYLADLH EAEAWIRERE PIVDNTNYGA
DEEAAGALLK KHEAFLVDLK AFGNSMQALR DQAEACQQQQ AAPVEEAARE ERVVALYDFQ
ARSPREVTMK KDDILTLLSS INKDWWKVEA DDQQGFVPAV YVRKLARDEF PMLPQRRREE
PGNITQRQEQ IENQYLSLLD RAEQRRRHLL QRYNEFLLAY EAGDMLDWIR EKKAENSGVE
LDDVWELQKK FDEFQMDLKT NEPRLRDINK VADDLQFEEL LTPEGAQIQQ ELNARWRSLQ
RLAEEQRQLL GSAHAVQMFH READDTKEQI EKKCQALSAA DPGSDLFSVQ ALQRQHEGFE
RDLIPLEEKV AVLGETADRL SESHPDATDD LQRQRLELNQ AWDDLLGLTE ERKENLQEDL
KFFLFLSQAR DQQNWLSGIG GMVSSQELAE DLTGTEIMIE RHQEHLAEME AEAPTFQALE
DFGTDLISSG HRASPKIEEE LQAVKLERDE LEKAWEQRKK MLDQCLELQF FRGNCDQAES
WMVVRENYLR SDDKGSLDSL EALMKKRDDL DKAITAQEKK ITELELFAEK LIADDHYAQE
EIAARRQRVL DRWKALKEQL IAERTKLGDY ADLKQFYHDL KDQEEWISEM LPIACDESYK
DPTNIQRKYL KHKTFENEVY GRAEQVKGVI TLGNTLIERR ACDGNEETMK GQVEELEKNW
DYLFERTIDK GQKLNEASRQ QRFNTGIRDF EFWLSEAETL LSMKDHARDL ASAGNLLKKH
QLLETEMLAR KDALKDLNTL AEDLISSGTF NTDQIVEKRD NVNERFLNVQ KLAAEHHEKL
KEAYALFQFF QDLDNEEFWI EEKLVRVRSQ DYGRDLQGVQ NLLKKHKRLE GELVAHEPII
QNVLDMAERL GDKAAVGREE IRERLDQFVQ HWDQLKELTK ARGIRLGESL EYLEFMANAE
EEEAWISEKE AMVTQGNSGD TLAATQSLLK KLEALENDFA VHEIRVQNVC AQGEDILSKE
ESQHKEKIST KIEALKEKTP SLAKAMAAWK LQLKDDYDFQ RFNWKADVVE AWIAEKETSL
KTNGNGADLA AFLTLLAKQD TLHASLQSFQ QERLSEITDL KDQLVAAEHS QTEAIKERHA
ALLRLWEQLL EASEAHRQEL LKKQLPLQKA EDLFMEFAHK ASAFNNWCEN AEEDLSEPVR
CISLDAIQQL KKDHEDFLAS LTRAQGDFNY LLELDQQIKA LNVSSSPYTW LTVEVLERIW
NHLSDIVKER EQELEKEESR QVKNFEMCQE FEQNASAFLD WIVQTRFLIW TSISRDYFLD
GSLLKETGTL ESQLEANKRK QKEIQAMKRK LTKIEDLGEN LEEALVLDIK YSTIGLAQQW
DQLYQLGMRR QHSLEEQIQA RDITGLSEET LQEFETAFRH FDENLTGRLS HKDFRSCLRG
LNYYLPMVEE GEPEPKFEKF LDAVDPGRKG YISQTDYTDF LIVKESENIK SSDELEDAFQ
ALAEGKAYIT KEDMKQALTP EQVSFCASHM QQYMDPRGRS QPAGYDYVGF ISSYFGK
//
