Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08032 (SPTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spectrin alpha chain, erythrocytic 1
Alternative name(s):
Erythroid alpha-spectrin
Gene names
Name:Spta1
Synonyms:Spna1, Spta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2415 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.

Subunit structure

Composed of non-homologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers. Interacts with FASLG By similarity.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex.

Miscellaneous

This complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin and mediates the binding of the whole complex to a transmembrane protein band 3. The interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for the regulation of plasma membrane components and for the maintenance of the lipid asymmetry of the plasma membrane.

Sequence similarities

Belongs to the spectrin family.

Contains 3 EF-hand domains.

Contains 1 SH3 domain.

Contains 21 spectrin repeats.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
SH3 domain
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionActin capping
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype PubMed 8195289. Source: MGI

actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

hemopoiesis

Inferred from mutant phenotype PubMed 11920196PubMed 6841965PubMed 7059672. Source: MGI

lymphocyte homeostasis

Inferred from mutant phenotype PubMed 1934076. Source: MGI

plasma membrane organization

Inferred from mutant phenotype PubMed 6841965. Source: MGI

porphyrin-containing compound biosynthetic process

Inferred from mutant phenotype PubMed 658175. Source: MGI

positive regulation of T cell proliferation

Inferred from mutant phenotype PubMed 7684329. Source: MGI

positive regulation of protein binding

Inferred from genetic interaction PubMed 20585040. Source: MGI

regulation of cell shape

Inferred from mutant phenotype PubMed 8195289. Source: MGI

   Cellular_componentcortical cytoskeleton

Inferred from direct assay PubMed 18723693. Source: MGI

cuticular plate

Inferred from direct assay PubMed 20016102. Source: MGI

membrane

Inferred from direct assay PubMed 18723693. Source: MGI

spectrin

Inferred from mutant phenotype PubMed 6234993. Source: MGI

spectrin-associated cytoskeleton

Inferred from mutant phenotype PubMed 6234993PubMed 6841965. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein heterodimerization activity

Inferred from physical interaction PubMed 20585040. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24152415Spectrin alpha chain, erythrocytic 1
PRO_0000073453

Regions

Repeat18 – 5033Spectrin 1
Repeat52 – 154103Spectrin 2
Repeat156 – 260105Spectrin 3
Repeat262 – 366105Spectrin 4
Repeat368 – 472105Spectrin 5
Repeat474 – 578105Spectrin 6
Repeat580 – 683104Spectrin 7
Repeat685 – 789105Spectrin 8
Repeat791 – 895105Spectrin 9
Repeat897 – 96670Spectrin 10
Domain975 – 103460SH3
Repeat1080 – 1179100Spectrin 11
Repeat1181 – 1285105Spectrin 12
Repeat1287 – 1391105Spectrin 13
Repeat1393 – 1496104Spectrin 14
Repeat1498 – 1603106Spectrin 15
Repeat1605 – 1709105Spectrin 16
Repeat1711 – 1815105Spectrin 17
Repeat1817 – 1922106Spectrin 18
Repeat1924 – 2029106Spectrin 19
Repeat2039 – 2143105Spectrin 20
Repeat2153 – 2254102Spectrin 21
Domain2267 – 230236EF-hand 1
Domain2310 – 234536EF-hand 2
Domain2347 – 238236EF-hand 3
Calcium binding2280 – 2291121 Potential
Calcium binding2323 – 2334122 Potential

Experimental info

Sequence conflict3371P → L in AAB47540. Ref.1
Sequence conflict5011D → Y in AAI50748. Ref.4
Sequence conflict7161G → V in AAB47540. Ref.1
Sequence conflict7411V → M in AAB47540. Ref.1
Sequence conflict7411V → M in AAI50748. Ref.4
Sequence conflict1044 – 10452RQ → QR in AAB47540. Ref.1
Sequence conflict1044 – 10452RQ → QR in AAI50748. Ref.4
Sequence conflict12251V → C in AAB47540. Ref.1
Sequence conflict12381T → N in AAB47540. Ref.1
Sequence conflict14251N → D in AAB47540. Ref.1
Sequence conflict15821K → M in AAB47540. Ref.1
Sequence conflict20621L → M in AAB47540. Ref.1
Sequence conflict20621L → M in AAI50748. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P08032 [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: 510B61CDEC4FAD13

FASTA2,415279,865
        10         20         30         40         50         60 
METPKETAVE SSGPKVLETA EEIQHRRAEV LNQYQRFKDR VAERGQKLEE SYHYQVFRRD 

        70         80         90        100        110        120 
ADDLEKWIME KLEIAKDKTY EPTNIQGKYQ KHESFVSEVQ AKSRVLPELE EIREARFAED 

       130        140        150        160        170        180 
HFAHEATKTH LKQLRLLWDL LLELTQEKSD VLLRALKFYQ YSQECEDILE WVKEKEAIVT 

       190        200        210        220        230        240 
LVELGDDWER TEVLHKKFEE FQEELTARKG KVDRVNQYAN ECAQEKHPKL PEIKAKQDEV 

       250        260        270        280        290        300 
NAAWDRLWSL ALKRRESLSN AADLQRFKRD VNEAIQWMEE KEPQLTSEDY GKDLVSSEAL 

       310        320        330        340        350        360 
FHNHKRLERN LAVMDDKVKE LCAKADKLMI SHSADAPQIQ QMKLDLVSNW ERIRALATNR 

       370        380        390        400        410        420 
YAKLKASYGY HRFLSDYDEL SGWMKEKTAL INADELPTDV ASGEALLARH QQHKHEIDSY 

       430        440        450        460        470        480 
DDRFQSADAT GQELLDGNHE ASEEIREKMT ILANDWAALL ELWDKCQHQY RQCLDFHLFY 

       490        500        510        520        530        540 
RDSEQVDSWM SRQEAFLENE DLGNSVGSVE ALLQKHDDFE EAFTAQEEKI ITLDETATKL 

       550        560        570        580        590        600 
IDNDHYDSEN IAAIRDGLLA RRDALRERAA TRRKLLVDSQ LLQQLYQDSD DLKTWINKKK 

       610        620        630        640        650        660 
KLADDDDYKD VQNLKSRVQK QQDFEEELAV NEIMLNNLEK TGQEMIEDGH YASEAVAARL 

       670        680        690        700        710        720 
SEVANLWKEL LEATAQKGTQ LYEANQLLQF ENNAEDLKRW LEEVEWQVTS EDYGKGLADV 

       730        740        750        760        770        780 
QNLLRKHGLL ESDVTARQNQ VDTLTDMAAH FEEIGHPDSG DIRARQESLL SRFEALKEPL 

       790        800        810        820        830        840 
AIRKKKLIDL LKLQQICRDS EDEEAWIQET EPSAASTHLG KDLVAAKNLL NRHEVILADI 

       850        860        870        880        890        900 
ASHEPRIQVI TERGNKMVEE GHFAAEDIAS RVESLNKNME SLHARAIRRE NDLKANVQLQ 

       910        920        930        940        950        960 
QYLADLHEAE AWIKEKEPIV DNKNYGADEE AAGALLKKHE AFLVDLNAFE NSIKALRDQA 

       970        980        990       1000       1010       1020 
EVCQQQQAAP VDEAGREARV IALYDFEARS RREVSMKKND VLTLLSSINK DWWKVEADDH 

      1030       1040       1050       1060       1070       1080 
QGFVPAVYVR KLAPDELPGF PQHRQEEPVN IPQLQQQVET LYHSLLDRAE ERRRRLLQRY 

      1090       1100       1110       1120       1130       1140 
NEFLLAYEAG DMLEWIQEKK TENTGVELDD VWELQKKFDE FQRDLKSNEP RLKDINKVAD 

      1150       1160       1170       1180       1190       1200 
ELLFEELLTP EGAHIRQELN TRWNSLKRLA DEQYQLLSSA HAVEMFHREA DDVKEQIDKK 

      1210       1220       1230       1240       1250       1260 
CRALNAADPG SDLLSVQALQ RQHEVFERDI IPLGEKVTTL GETAERLCES HPDATEDLQK 

      1270       1280       1290       1300       1310       1320 
QRTELNEAWD TLQGLTSDRK ESLNEAHKFF LFLSKASDLE NWIKTIGGVI SSPELAEDLT 

      1330       1340       1350       1360       1370       1380 
GTEILLERHQ EHHDDIKRED PTFQALEDFG TELIDSGHRN RREIDNTLQN INSKRDNLEK 

      1390       1400       1410       1420       1430       1440 
SWENRKKMLD QCLELQLFRG KCDQVESWMV ARENSLRSDD RDHLNSLQAL MKKRDDLDKA 

      1450       1460       1470       1480       1490       1500 
ITAQEGKISD LENVATRLID NDHYAKEEIA ARLQRVLDRW KALKEQLLTE LGKLGDYADL 

      1510       1520       1530       1540       1550       1560 
KQFYRDLEDL EEWINEMLPI ACDESYKDPT NIQRKYLKHQ AFENEVNGRA EQVDGVINLG 

      1570       1580       1590       1600       1610       1620 
NSLIERRVCD GDEENMQEQL DKLKENWDYL LERTTDKGQK LNEASRQQRF NTSIRDFEFW 

      1630       1640       1650       1660       1670       1680 
LSEAEGLLAM KDQARDLTSA GNLLKKHQLL EAEMLAREDP LKDLNDLAQE LISSGTFNID 

      1690       1700       1710       1720       1730       1740 
QIEEKMNGVN ERFENVQSLA AAHHEKLKET YALFQFFQDL DDEEAWIEEK LLRVSSQDYG 

      1750       1760       1770       1780       1790       1800 
RDLQSVQNLL KKHKRLEGEL VAHEPAVQNV LDTAESLRDK AAVGKEEIQE RLAQFVQHWE 

      1810       1820       1830       1840       1850       1860 
KLKELAKTRG VNLEESLEYL QFMENAEEEE AWLGEKCALV SRGDSGDTLA ATQSLLKKHE 

      1870       1880       1890       1900       1910       1920 
ALENDFAVHK NRVQDVCAQG EDILNKEETQ NKDKISTKIQ VLNEKTASLA KALAAWKSQL 

      1930       1940       1950       1960       1970       1980 
DDVHAFQQFN WKADVVESWI GEKEASLKTK SNGADLTAFL TLLAKHDTLD ASLQSFQQER 

      1990       2000       2010       2020       2030       2040 
LSEIAELKDQ LVAGEHSQAK AIEEQHAALL RHWEQLLEAS RVHRQKLLEK QLPLQKAEEL 

      2050       2060       2070       2080       2090       2100 
FMEFAHKASA FNNWCENAEE DLSEPVHCVS LNEIRQLQKE HEAFLASLAG AQEDFNYLLE 

      2110       2120       2130       2140       2150       2160 
LDKQIKALNV PSSPYTWLTV DVLGRIWNHL PDIIKEREQE LQKEEARQIK NFEMCQEFEQ 

      2170       2180       2190       2200       2210       2220 
NASAFLQWIQ ETRAYFLDGS LLKETGTLES QLEANKRKQK EIQAMKRHLT KIEDLGDSME 

      2230       2240       2250       2260       2270       2280 
EALILDIKYS TIGLAQQWDQ LHQLGMRMQH NLEQQIQAKD TIGVSEETLK EFSTTYKHFD 

      2290       2300       2310       2320       2330       2340 
ENLTGRLTHK EFRSCLRGLN YYLPMVEEGE PEPKFEKFLN AVDPGRKGYV SLEDYTSFLI 

      2350       2360       2370       2380       2390       2400 
DKESENIKTS DDIESAFQAL AEGKAYITKE DMKQALTPEQ VSFCTIHMQQ YMDPRGRSQP 

      2410 
AGYDYVGFTN SFFGN 

« Hide

References

« Hide 'large scale' references
[1]Burnett R.C., Avery A.C., Swardson C.J.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/cJ.
[2]Birkenmeier C.S., Gifford E.J., Barker J.E.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Sequence comparison of human and murine erythrocyte alpha-spectrin cDNA."
Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P., Shane S., Rovera G.
Gene 36:357-362(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1567-1819.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87455 mRNA. Translation: AAB47540.1.
AF093576 mRNA. Translation: AAC61874.1.
AC113483 mRNA. No translation available.
AC156549 mRNA. No translation available.
BC150747 mRNA. Translation: AAI50748.1.
M10276 mRNA. Translation: AAA40123.1.
PIRA05283.
RefSeqNP_035595.2. NM_011465.4.
UniGeneMm.200611.

3D structure databases

ProteinModelPortalP08032.
SMRP08032. Positions 4-2260, 2263-2415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203458. 5 interactions.
IntActP08032. 2 interactions.
MINTMINT-85326.

PTM databases

PhosphoSiteP08032.

Proteomic databases

PaxDbP08032.
PRIDEP08032.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027817; ENSMUSP00000027817; ENSMUSG00000026532.
GeneID20739.
KEGGmmu:20739.
UCSCuc007dsw.2. mouse.

Organism-specific databases

CTD6708.
MGIMGI:98385. Spta1.

Phylogenomic databases

eggNOGNOG237318.
GeneTreeENSGT00750000117361.
HOGENOMHOG000246965.
HOVERGENHBG059266.
InParanoidB2RWX6.
KOK06114.
OMASINKDWW.
OrthoDBEOG7GXP9K.
PhylomeDBP08032.
TreeFamTF343803.

Gene expression databases

BgeeP08032.
CleanExMM_SPNA1.
GenevestigatorP08032.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSPR01887. SPECTRNALPHA.
SMARTSM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299373.
PROP08032.
SOURCESearch...

Entry information

Entry nameSPTA1_MOUSE
AccessionPrimary (citable) accession number: P08032
Secondary accession number(s): B2RWX6, P97502
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 7, 2009
Last modified: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot