SPTA1_MOUSE
ID SPTA1_MOUSE Reviewed; 2415 AA.
AC P08032; B2RWX6; P97502;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Spectrin alpha chain, erythrocytic 1;
DE AltName: Full=Erythroid alpha-spectrin;
GN Name=Spta1; Synonyms=Spna1, Spta;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Burnett R.C., Avery A.C., Swardson C.J.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Birkenmeier C.S., Gifford E.J., Barker J.E.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1567-1819.
RX PubMed=3000887; DOI=10.1016/0378-1119(85)90191-x;
RA Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P., Shane S.,
RA Rovera G.;
RT "Sequence comparison of human and murine erythrocyte alpha-spectrin cDNA.";
RL Gene 36:357-362(1985).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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).
CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal network
CC underlying the erythrocyte plasma membrane. It associates with band 4.1
CC and actin to form the cytoskeletal superstructure of the erythrocyte
CC plasma membrane.
CC -!- SUBUNIT: Composed of non-homologous chains, alpha and beta, which
CC aggregate to form dimers, tetramers, and higher polymers. Interacts
CC with FASLG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of the
CC plasma membrane via another protein, ankyrin, which binds to beta-
CC spectrin and mediates the binding of the whole complex to a
CC transmembrane protein band 3. The interaction of erythrocyte spectrin
CC with other proteins through specific binding domains lead to the
CC formation of an extensive subplasmalemmal meshwork which is thought to
CC be responsible for the maintenance of the biconcave shape of human
CC erythrocytes, for the regulation of plasma membrane components and for
CC the maintenance of the lipid asymmetry of the plasma membrane.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
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 EMBL; U87455; AAB47540.1; -; mRNA.
DR EMBL; AF093576; AAC61874.1; -; mRNA.
DR EMBL; AC113483; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC156549; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC150747; AAI50748.1; -; mRNA.
DR EMBL; M10276; AAA40123.1; -; mRNA.
DR CCDS; CCDS35795.1; -.
DR PIR; A05283; A05283.
DR RefSeq; NP_035595.2; NM_011465.4.
DR AlphaFoldDB; P08032; -.
DR SMR; P08032; -.
DR BioGRID; 203458; 9.
DR IntAct; P08032; 6.
DR MINT; P08032; -.
DR STRING; 10090.ENSMUSP00000027817; -.
DR iPTMnet; P08032; -.
DR PhosphoSitePlus; P08032; -.
DR SwissPalm; P08032; -.
DR EPD; P08032; -.
DR jPOST; P08032; -.
DR MaxQB; P08032; -.
DR PaxDb; P08032; -.
DR PeptideAtlas; P08032; -.
DR PRIDE; P08032; -.
DR ProteomicsDB; 261579; -.
DR Antibodypedia; 10818; 177 antibodies from 28 providers.
DR DNASU; 20739; -.
DR Ensembl; ENSMUST00000027817; ENSMUSP00000027817; ENSMUSG00000026532.
DR GeneID; 20739; -.
DR KEGG; mmu:20739; -.
DR UCSC; uc007dsw.2; mouse.
DR CTD; 6708; -.
DR MGI; MGI:98385; Spta1.
DR VEuPathDB; HostDB:ENSMUSG00000026532; -.
DR eggNOG; KOG0040; Eukaryota.
DR GeneTree; ENSGT00940000161240; -.
DR HOGENOM; CLU_000847_0_0_1; -.
DR InParanoid; P08032; -.
DR OMA; DYKDTQN; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; P08032; -.
DR TreeFam; TF343803; -.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR BioGRID-ORCS; 20739; 2 hits in 72 CRISPR screens.
DR PRO; PR:P08032; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P08032; protein.
DR Bgee; ENSMUSG00000026532; Expressed in fetal liver hematopoietic progenitor cell and 79 other tissues.
DR Genevisible; P08032; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008091; C:spectrin; IMP:MGI.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IMP:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IMP:MGI.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IGI:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR CDD; cd00176; SPEC; 11.
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 Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cell shape; Cytoplasm; Cytoskeleton;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2415
FT /note="Spectrin alpha chain, erythrocytic 1"
FT /id="PRO_0000073453"
FT REPEAT 52..152
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 157..259
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 263..365
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 370..471
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 475..576
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 580..681
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 686..787
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 792..894
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 898..967
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 975..1034
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1085..1177
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1183..1285
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1287..1390
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1394..1489
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1499..1603
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1606..1709
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1712..1815
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 1818..1921
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1924..2029
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2040..2142
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2154..2254
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2267..2302
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2310..2345
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2347..2382
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 2323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 2329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 2334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02549"
FT MOD_RES 1972
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02549"
FT CONFLICT 337
FT /note="P -> L (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="D -> Y (in Ref. 4; AAI50748)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="G -> V (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="V -> M (in Ref. 1; AAB47540 and 4; AAI50748)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044..1045
FT /note="RQ -> QR (in Ref. 1; AAB47540 and 4; AAI50748)"
FT /evidence="ECO:0000305"
FT CONFLICT 1225
FT /note="V -> C (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="T -> N (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1425
FT /note="N -> D (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1582
FT /note="K -> M (in Ref. 1; AAB47540)"
FT /evidence="ECO:0000305"
FT CONFLICT 2062
FT /note="L -> M (in Ref. 1; AAB47540 and 4; AAI50748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2415 AA; 279865 MW; 510B61CDEC4FAD13 CRC64;
METPKETAVE SSGPKVLETA EEIQHRRAEV LNQYQRFKDR VAERGQKLEE SYHYQVFRRD
ADDLEKWIME KLEIAKDKTY EPTNIQGKYQ KHESFVSEVQ AKSRVLPELE EIREARFAED
HFAHEATKTH LKQLRLLWDL LLELTQEKSD VLLRALKFYQ YSQECEDILE WVKEKEAIVT
LVELGDDWER TEVLHKKFEE FQEELTARKG KVDRVNQYAN ECAQEKHPKL PEIKAKQDEV
NAAWDRLWSL ALKRRESLSN AADLQRFKRD VNEAIQWMEE KEPQLTSEDY GKDLVSSEAL
FHNHKRLERN LAVMDDKVKE LCAKADKLMI SHSADAPQIQ QMKLDLVSNW ERIRALATNR
YAKLKASYGY HRFLSDYDEL SGWMKEKTAL INADELPTDV ASGEALLARH QQHKHEIDSY
DDRFQSADAT GQELLDGNHE ASEEIREKMT ILANDWAALL ELWDKCQHQY RQCLDFHLFY
RDSEQVDSWM SRQEAFLENE DLGNSVGSVE ALLQKHDDFE EAFTAQEEKI ITLDETATKL
IDNDHYDSEN IAAIRDGLLA RRDALRERAA TRRKLLVDSQ LLQQLYQDSD DLKTWINKKK
KLADDDDYKD VQNLKSRVQK QQDFEEELAV NEIMLNNLEK TGQEMIEDGH YASEAVAARL
SEVANLWKEL LEATAQKGTQ LYEANQLLQF ENNAEDLKRW LEEVEWQVTS EDYGKGLADV
QNLLRKHGLL ESDVTARQNQ VDTLTDMAAH FEEIGHPDSG DIRARQESLL SRFEALKEPL
AIRKKKLIDL LKLQQICRDS EDEEAWIQET EPSAASTHLG KDLVAAKNLL NRHEVILADI
ASHEPRIQVI TERGNKMVEE GHFAAEDIAS RVESLNKNME SLHARAIRRE NDLKANVQLQ
QYLADLHEAE AWIKEKEPIV DNKNYGADEE AAGALLKKHE AFLVDLNAFE NSIKALRDQA
EVCQQQQAAP VDEAGREARV IALYDFEARS RREVSMKKND VLTLLSSINK DWWKVEADDH
QGFVPAVYVR KLAPDELPGF PQHRQEEPVN IPQLQQQVET LYHSLLDRAE ERRRRLLQRY
NEFLLAYEAG DMLEWIQEKK TENTGVELDD VWELQKKFDE FQRDLKSNEP RLKDINKVAD
ELLFEELLTP EGAHIRQELN TRWNSLKRLA DEQYQLLSSA HAVEMFHREA DDVKEQIDKK
CRALNAADPG SDLLSVQALQ RQHEVFERDI IPLGEKVTTL GETAERLCES HPDATEDLQK
QRTELNEAWD TLQGLTSDRK ESLNEAHKFF LFLSKASDLE NWIKTIGGVI SSPELAEDLT
GTEILLERHQ EHHDDIKRED PTFQALEDFG TELIDSGHRN RREIDNTLQN INSKRDNLEK
SWENRKKMLD QCLELQLFRG KCDQVESWMV ARENSLRSDD RDHLNSLQAL MKKRDDLDKA
ITAQEGKISD LENVATRLID NDHYAKEEIA ARLQRVLDRW KALKEQLLTE LGKLGDYADL
KQFYRDLEDL EEWINEMLPI ACDESYKDPT NIQRKYLKHQ AFENEVNGRA EQVDGVINLG
NSLIERRVCD GDEENMQEQL DKLKENWDYL LERTTDKGQK LNEASRQQRF NTSIRDFEFW
LSEAEGLLAM KDQARDLTSA GNLLKKHQLL EAEMLAREDP LKDLNDLAQE LISSGTFNID
QIEEKMNGVN ERFENVQSLA AAHHEKLKET YALFQFFQDL DDEEAWIEEK LLRVSSQDYG
RDLQSVQNLL KKHKRLEGEL VAHEPAVQNV LDTAESLRDK AAVGKEEIQE RLAQFVQHWE
KLKELAKTRG VNLEESLEYL QFMENAEEEE AWLGEKCALV SRGDSGDTLA ATQSLLKKHE
ALENDFAVHK NRVQDVCAQG EDILNKEETQ NKDKISTKIQ VLNEKTASLA KALAAWKSQL
DDVHAFQQFN WKADVVESWI GEKEASLKTK SNGADLTAFL TLLAKHDTLD ASLQSFQQER
LSEIAELKDQ LVAGEHSQAK AIEEQHAALL RHWEQLLEAS RVHRQKLLEK QLPLQKAEEL
FMEFAHKASA FNNWCENAEE DLSEPVHCVS LNEIRQLQKE HEAFLASLAG AQEDFNYLLE
LDKQIKALNV PSSPYTWLTV DVLGRIWNHL PDIIKEREQE LQKEEARQIK NFEMCQEFEQ
NASAFLQWIQ ETRAYFLDGS LLKETGTLES QLEANKRKQK EIQAMKRHLT KIEDLGDSME
EALILDIKYS TIGLAQQWDQ LHQLGMRMQH NLEQQIQAKD TIGVSEETLK EFSTTYKHFD
ENLTGRLTHK EFRSCLRGLN YYLPMVEEGE PEPKFEKFLN AVDPGRKGYV SLEDYTSFLI
DKESENIKTS DDIESAFQAL AEGKAYITKE DMKQALTPEQ VSFCTIHMQQ YMDPRGRSQP
AGYDYVGFTN SFFGN
