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Database: UniProt
Entry: U3JFB7_FICAL
LinkDB: U3JFB7_FICAL
Original site: U3JFB7_FICAL 
ID   U3JFB7_FICAL            Unreviewed;      2471 AA.
AC   U3JFB7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Spectrin alpha, non-erythrocytic 1 {ECO:0000313|Ensembl:ENSFALP00000001471.2};
GN   Name=SPTAN1 {ECO:0000313|Ensembl:ENSFALP00000001471.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001471.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000001471.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000001471.2}
RP   IDENTIFICATION.
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; ENSFALT00000001480.2; ENSFALP00000001471.2; ENSFALG00000001408.2.
DR   GeneTree; ENSGT00940000156662; -.
DR   HOGENOM; CLU_000847_0_0_1; -.
DR   OrthoDB; 2872403at2759; -.
DR   Proteomes; UP000016665; 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; PH_9 DOMAIN-CONTAINING PROTEIN-RELATED; 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; 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:UP000016665};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          2322..2357
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          2365..2400
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          1126..1160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1698..1732
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2177..2209
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2471 AA;  284613 MW;  E80ED427FE3FDADF CRC64;
     MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ RDADELEKWI
     QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV 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 NQTLITKEVG SVSLRMKQVE ELYHSLLELG
     EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL
     KANESRLKDI NKVAKDLESE GLMADEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH
     TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN
     YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL QEKCTELNQA
     WNSLGKRADQ RKEKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
     HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM
     LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
     IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWLRLKAQM IEKRSKLGES QTLQQFSRDV
     DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS
     LIERGACAGS EDAVKARLAA LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS
     EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV
     KDKRETINGR FQRIKGMASA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD
     LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL AQFVDHWKEL
     KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF
     ETDFTVHKDR VNDVCANGED LIKKNNHHEA NITAKMKGLR GKVSDLEKAA AQRKAKLDEN
     SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN
     ITALKDQLLA AKHIQSKAIE ARHASLMKRW NQLLANSATR KKKLLEAQEH FRKVEDLFLT
     FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR
     QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN
     AFHQWIQETR SCMVEESGTL ESQLEATKRK HQEIRAMRSQ LKKIEDLGAA MEEALILDNK
     YTEHSTVGLA QQWDQLDQLG MRMQHNLEQQ IQARNTTGVT EEALKEFSMM FKHFDKDKSG
     RLNHQEFKSC LRSLGYDLPM VEEGEPDPEF ESILDTVDPN RDGHVSLQEY MAFMISRETE
     NVKSSEEIES AFRALSSEGK PYVTKEELYQ NLTREQADYC ISHMKPYMDG KGRELPSAYD
     YIEFTRSLFV N
//
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