ID E9Q447_MOUSE Unreviewed; 2478 AA.
AC E9Q447;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Spectrin alpha, non-erythrocytic 1 {ECO:0000313|Ensembl:ENSMUSP00000109348.3};
GN Name=Sptan1 {ECO:0000313|Ensembl:ENSMUSP00000109348.3,
GN ECO:0000313|MGI:MGI:98386};
GN Synonyms=Spna2 {ECO:0000313|MGI:MGI:98386};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000109348.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [2] {ECO:0007829|PubMed:17114649}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [3] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000109348.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109348.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7] {ECO:0000313|Ensembl:ENSMUSP00000109348.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109348.3};
RG Ensembl;
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 SMR; E9Q447; -.
DR iPTMnet; E9Q447; -.
DR jPOST; E9Q447; -.
DR MaxQB; E9Q447; -.
DR PeptideAtlas; E9Q447; -.
DR ProteomicsDB; 314666; -.
DR Antibodypedia; 1910; 572 antibodies from 44 providers.
DR Ensembl; ENSMUST00000113719.9; ENSMUSP00000109348.3; ENSMUSG00000057738.15.
DR UCSC; uc008jar.1; mouse.
DR AGR; MGI:98386; -.
DR MGI; MGI:98386; Sptan1.
DR VEuPathDB; HostDB:ENSMUSG00000057738; -.
DR GeneTree; ENSGT00940000156662; -.
DR PhylomeDB; E9Q447; -.
DR ChiTaRS; Sptan1; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000057738; Expressed in facial nucleus and 274 other cell types or tissues.
DR ExpressionAtlas; E9Q447; baseline and differential.
DR Genevisible; E9Q447; MM.
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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:E9Q447,
KW ECO:0007829|MaxQB:E9Q447};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 2329..2364
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2372..2407
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 858..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1106..1140
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1678..1712
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2157..2189
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2478 AA; 285345 MW; FB9ED04A506CCF22 CRC64;
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI
QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD
LEHVEVLQKK FEEFQTDLAA HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL
KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA AERHARLDDS
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA
DESGQALLAA SHYASDEVRE KLSILSEERT ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQSA SRENLLEEQG SIALRQGQID NQYQSLLELG EKRKGMLEKS CKKFMLFREA
NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI NKVAEDLESE
GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH TVATFNSIKE LNERWRSLQQ
LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN YGHDLASVQA LQRKHEGFER
DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA WTSLGKRADQ RKAKLGDSHD
LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ
FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDHCLELQLF HRDCEQAENW
MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK IAALQAFADQ LIAVDHYAKG
DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV DEIEAWISEK LQTASDESYK
DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS LIERGACAGS EDAVKARLAA
LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS EVEALLASED YGKDLASVNN
LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV KEKRDTINGR FQKIKSMATS
RRAKLSESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD LTGVQNLRKK HKRLEAELAA
HEPAIQGVLD TGKKLSDDNT IGQEEIQQRL AQFVEHWKEL KQLAAARGQR LEESLEYQQF
VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF ETDFTVHKDR VNDVCTNGQD
LIKKNNHHEE NISSKMKGLN GKVSDLEKAA AQRKAKLDEN SAFLQFNWKA DVVESWIGEK
ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN ITALKDQLLA AKHIQSKAIE
ARHASLMKRW TQLLANSATR KKKLLEAQSH FRKVEDLFLT FAKKASAFNS WFENAEEDLT
DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR QIKSFRVASN PYTWFTMEAL
EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN AFHQWIQETR TYLLDGIAYR
RVIRVCQYEV GDDLSGRSCM VEESGTLESQ LEATKRKHQE IRAMRSQLKK IEDLGAAMEE
ALILDNKYTE HSTVGLAQQW DQLDQLGMRM QHNLEQQIQA RNTTGVTEEA LKEFSMMFKH
FDKDKSGRLN HQEFKSCLRS LGYDLPMVEE GEPDPEFEAI LDTVDPNRDG HVSLQEYMAF
MISRETENVK SSEEIESAFR ALSSEGKPYV TKEELYQNLT REQADYCVSH MKPYVDGKGR
ELPTAFDYVE FTRSLFVN
//
