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P08032

- SPTA1_MOUSE

UniProt

P08032 - SPTA1_MOUSE

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Protein

Spectrin alpha chain, erythrocytic 1

Gene

Spta1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2280 – 2291121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi2323 – 2334122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein heterodimerization activity Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. actin filament capping Source: UniProtKB-KW
  3. hemopoiesis Source: MGI
  4. lymphocyte homeostasis Source: MGI
  5. plasma membrane organization Source: MGI
  6. porphyrin-containing compound biosynthetic process Source: MGI
  7. positive regulation of protein binding Source: MGI
  8. positive regulation of T cell proliferation Source: MGI
  9. regulation of cell shape Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cell shape

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain, erythrocytic 1
Alternative name(s):
Erythroid alpha-spectrin
Gene namesi
Name:Spta1
Synonyms:Spna1, Spta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:98385. Spta1.

Subcellular locationi

GO - Cellular componenti

  1. cortical cytoskeleton Source: MGI
  2. cuticular plate Source: MGI
  3. membrane Source: MGI
  4. spectrin Source: MGI
  5. spectrin-associated cytoskeleton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24152415Spectrin alpha chain, erythrocytic 1PRO_0000073453Add
BLAST

Proteomic databases

MaxQBiP08032.
PaxDbiP08032.
PRIDEiP08032.

PTM databases

PhosphoSiteiP08032.

Expressioni

Gene expression databases

BgeeiP08032.
CleanExiMM_SPNA1.
GenevestigatoriP08032.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi203458. 5 interactions.
IntActiP08032. 2 interactions.
MINTiMINT-85326.

Structurei

3D structure databases

ProteinModelPortaliP08032.
SMRiP08032. Positions 4-953, 992-1032, 1047-2260, 2263-2411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 5033Spectrin 1Add
BLAST
Repeati52 – 154103Spectrin 2Add
BLAST
Repeati156 – 260105Spectrin 3Add
BLAST
Repeati262 – 366105Spectrin 4Add
BLAST
Repeati368 – 472105Spectrin 5Add
BLAST
Repeati474 – 578105Spectrin 6Add
BLAST
Repeati580 – 683104Spectrin 7Add
BLAST
Repeati685 – 789105Spectrin 8Add
BLAST
Repeati791 – 895105Spectrin 9Add
BLAST
Repeati897 – 96670Spectrin 10Add
BLAST
Domaini975 – 103460SH3PROSITE-ProRule annotationAdd
BLAST
Repeati1080 – 1179100Spectrin 11Add
BLAST
Repeati1181 – 1285105Spectrin 12Add
BLAST
Repeati1287 – 1391105Spectrin 13Add
BLAST
Repeati1393 – 1496104Spectrin 14Add
BLAST
Repeati1498 – 1603106Spectrin 15Add
BLAST
Repeati1605 – 1709105Spectrin 16Add
BLAST
Repeati1711 – 1815105Spectrin 17Add
BLAST
Repeati1817 – 1922106Spectrin 18Add
BLAST
Repeati1924 – 2029106Spectrin 19Add
BLAST
Repeati2039 – 2143105Spectrin 20Add
BLAST
Repeati2153 – 2254102Spectrin 21Add
BLAST
Domaini2267 – 230236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini2310 – 234536EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini2347 – 238236EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 21 spectrin repeats.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG237318.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000246965.
HOVERGENiHBG059266.
InParanoidiP08032.
KOiK06114.
OMAiSINKDWW.
OrthoDBiEOG7GXP9K.
PhylomeDBiP08032.
TreeFamiTF343803.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. 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]
PfamiPF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSiPR01887. SPECTRNALPHA.
SMARTiSM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08032-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
METPKETAVE SSGPKVLETA EEIQHRRAEV LNQYQRFKDR VAERGQKLEE
60 70 80 90 100
SYHYQVFRRD ADDLEKWIME KLEIAKDKTY EPTNIQGKYQ KHESFVSEVQ
110 120 130 140 150
AKSRVLPELE EIREARFAED HFAHEATKTH LKQLRLLWDL LLELTQEKSD
160 170 180 190 200
VLLRALKFYQ YSQECEDILE WVKEKEAIVT LVELGDDWER TEVLHKKFEE
210 220 230 240 250
FQEELTARKG KVDRVNQYAN ECAQEKHPKL PEIKAKQDEV NAAWDRLWSL
260 270 280 290 300
ALKRRESLSN AADLQRFKRD VNEAIQWMEE KEPQLTSEDY GKDLVSSEAL
310 320 330 340 350
FHNHKRLERN LAVMDDKVKE LCAKADKLMI SHSADAPQIQ QMKLDLVSNW
360 370 380 390 400
ERIRALATNR YAKLKASYGY HRFLSDYDEL SGWMKEKTAL INADELPTDV
410 420 430 440 450
ASGEALLARH QQHKHEIDSY DDRFQSADAT GQELLDGNHE ASEEIREKMT
460 470 480 490 500
ILANDWAALL ELWDKCQHQY RQCLDFHLFY RDSEQVDSWM SRQEAFLENE
510 520 530 540 550
DLGNSVGSVE ALLQKHDDFE EAFTAQEEKI ITLDETATKL IDNDHYDSEN
560 570 580 590 600
IAAIRDGLLA RRDALRERAA TRRKLLVDSQ LLQQLYQDSD DLKTWINKKK
610 620 630 640 650
KLADDDDYKD VQNLKSRVQK QQDFEEELAV NEIMLNNLEK TGQEMIEDGH
660 670 680 690 700
YASEAVAARL SEVANLWKEL LEATAQKGTQ LYEANQLLQF ENNAEDLKRW
710 720 730 740 750
LEEVEWQVTS EDYGKGLADV QNLLRKHGLL ESDVTARQNQ VDTLTDMAAH
760 770 780 790 800
FEEIGHPDSG DIRARQESLL SRFEALKEPL AIRKKKLIDL LKLQQICRDS
810 820 830 840 850
EDEEAWIQET EPSAASTHLG KDLVAAKNLL NRHEVILADI ASHEPRIQVI
860 870 880 890 900
TERGNKMVEE GHFAAEDIAS RVESLNKNME SLHARAIRRE NDLKANVQLQ
910 920 930 940 950
QYLADLHEAE AWIKEKEPIV DNKNYGADEE AAGALLKKHE AFLVDLNAFE
960 970 980 990 1000
NSIKALRDQA EVCQQQQAAP VDEAGREARV IALYDFEARS RREVSMKKND
1010 1020 1030 1040 1050
VLTLLSSINK DWWKVEADDH QGFVPAVYVR KLAPDELPGF PQHRQEEPVN
1060 1070 1080 1090 1100
IPQLQQQVET LYHSLLDRAE ERRRRLLQRY NEFLLAYEAG DMLEWIQEKK
1110 1120 1130 1140 1150
TENTGVELDD VWELQKKFDE FQRDLKSNEP RLKDINKVAD ELLFEELLTP
1160 1170 1180 1190 1200
EGAHIRQELN TRWNSLKRLA DEQYQLLSSA HAVEMFHREA DDVKEQIDKK
1210 1220 1230 1240 1250
CRALNAADPG SDLLSVQALQ RQHEVFERDI IPLGEKVTTL GETAERLCES
1260 1270 1280 1290 1300
HPDATEDLQK QRTELNEAWD TLQGLTSDRK ESLNEAHKFF LFLSKASDLE
1310 1320 1330 1340 1350
NWIKTIGGVI SSPELAEDLT GTEILLERHQ EHHDDIKRED PTFQALEDFG
1360 1370 1380 1390 1400
TELIDSGHRN RREIDNTLQN INSKRDNLEK SWENRKKMLD QCLELQLFRG
1410 1420 1430 1440 1450
KCDQVESWMV ARENSLRSDD RDHLNSLQAL MKKRDDLDKA ITAQEGKISD
1460 1470 1480 1490 1500
LENVATRLID NDHYAKEEIA ARLQRVLDRW KALKEQLLTE LGKLGDYADL
1510 1520 1530 1540 1550
KQFYRDLEDL EEWINEMLPI ACDESYKDPT NIQRKYLKHQ AFENEVNGRA
1560 1570 1580 1590 1600
EQVDGVINLG NSLIERRVCD GDEENMQEQL DKLKENWDYL LERTTDKGQK
1610 1620 1630 1640 1650
LNEASRQQRF NTSIRDFEFW LSEAEGLLAM KDQARDLTSA GNLLKKHQLL
1660 1670 1680 1690 1700
EAEMLAREDP LKDLNDLAQE LISSGTFNID QIEEKMNGVN ERFENVQSLA
1710 1720 1730 1740 1750
AAHHEKLKET YALFQFFQDL DDEEAWIEEK LLRVSSQDYG RDLQSVQNLL
1760 1770 1780 1790 1800
KKHKRLEGEL VAHEPAVQNV LDTAESLRDK AAVGKEEIQE RLAQFVQHWE
1810 1820 1830 1840 1850
KLKELAKTRG VNLEESLEYL QFMENAEEEE AWLGEKCALV SRGDSGDTLA
1860 1870 1880 1890 1900
ATQSLLKKHE ALENDFAVHK NRVQDVCAQG EDILNKEETQ NKDKISTKIQ
1910 1920 1930 1940 1950
VLNEKTASLA KALAAWKSQL DDVHAFQQFN WKADVVESWI GEKEASLKTK
1960 1970 1980 1990 2000
SNGADLTAFL TLLAKHDTLD ASLQSFQQER LSEIAELKDQ LVAGEHSQAK
2010 2020 2030 2040 2050
AIEEQHAALL RHWEQLLEAS RVHRQKLLEK QLPLQKAEEL FMEFAHKASA
2060 2070 2080 2090 2100
FNNWCENAEE DLSEPVHCVS LNEIRQLQKE HEAFLASLAG AQEDFNYLLE
2110 2120 2130 2140 2150
LDKQIKALNV PSSPYTWLTV DVLGRIWNHL PDIIKEREQE LQKEEARQIK
2160 2170 2180 2190 2200
NFEMCQEFEQ NASAFLQWIQ ETRAYFLDGS LLKETGTLES QLEANKRKQK
2210 2220 2230 2240 2250
EIQAMKRHLT KIEDLGDSME EALILDIKYS TIGLAQQWDQ LHQLGMRMQH
2260 2270 2280 2290 2300
NLEQQIQAKD TIGVSEETLK EFSTTYKHFD ENLTGRLTHK EFRSCLRGLN
2310 2320 2330 2340 2350
YYLPMVEEGE PEPKFEKFLN AVDPGRKGYV SLEDYTSFLI DKESENIKTS
2360 2370 2380 2390 2400
DDIESAFQAL AEGKAYITKE DMKQALTPEQ VSFCTIHMQQ YMDPRGRSQP
2410
AGYDYVGFTN SFFGN
Length:2,415
Mass (Da):279,865
Last modified:July 7, 2009 - v3
Checksum:i510B61CDEC4FAD13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3371P → L in AAB47540. 1 PublicationCurated
Sequence conflicti501 – 5011D → Y in AAI50748. (PubMed:15489334)Curated
Sequence conflicti716 – 7161G → V in AAB47540. 1 PublicationCurated
Sequence conflicti741 – 7411V → M in AAB47540. 1 PublicationCurated
Sequence conflicti741 – 7411V → M in AAI50748. (PubMed:15489334)Curated
Sequence conflicti1044 – 10452RQ → QR in AAB47540. 1 PublicationCurated
Sequence conflicti1044 – 10452RQ → QR in AAI50748. (PubMed:15489334)Curated
Sequence conflicti1225 – 12251V → C in AAB47540. 1 PublicationCurated
Sequence conflicti1238 – 12381T → N in AAB47540. 1 PublicationCurated
Sequence conflicti1425 – 14251N → D in AAB47540. 1 PublicationCurated
Sequence conflicti1582 – 15821K → M in AAB47540. 1 PublicationCurated
Sequence conflicti2062 – 20621L → M in AAB47540. 1 PublicationCurated
Sequence conflicti2062 – 20621L → M in AAI50748. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35795.1.
PIRiA05283.
RefSeqiNP_035595.2. NM_011465.4.
UniGeneiMm.200611.

Genome annotation databases

EnsembliENSMUST00000027817; ENSMUSP00000027817; ENSMUSG00000026532.
GeneIDi20739.
KEGGimmu:20739.
UCSCiuc007dsw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35795.1.
PIRi A05283.
RefSeqi NP_035595.2. NM_011465.4.
UniGenei Mm.200611.

3D structure databases

ProteinModelPortali P08032.
SMRi P08032. Positions 4-953, 992-1032, 1047-2260, 2263-2411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203458. 5 interactions.
IntActi P08032. 2 interactions.
MINTi MINT-85326.

PTM databases

PhosphoSitei P08032.

Proteomic databases

MaxQBi P08032.
PaxDbi P08032.
PRIDEi P08032.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027817 ; ENSMUSP00000027817 ; ENSMUSG00000026532 .
GeneIDi 20739.
KEGGi mmu:20739.
UCSCi uc007dsw.2. mouse.

Organism-specific databases

CTDi 6708.
MGIi MGI:98385. Spta1.

Phylogenomic databases

eggNOGi NOG237318.
GeneTreei ENSGT00760000118813.
HOGENOMi HOG000246965.
HOVERGENi HBG059266.
InParanoidi P08032.
KOi K06114.
OMAi SINKDWW.
OrthoDBi EOG7GXP9K.
PhylomeDBi P08032.
TreeFami TF343803.

Miscellaneous databases

NextBioi 299373.
PROi P08032.
SOURCEi Search...

Gene expression databases

Bgeei P08032.
CleanExi MM_SPNA1.
Genevestigatori P08032.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. 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 ]
Pfami PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view ]
PRINTSi PR01887. SPECTRNALPHA.
SMARTi SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSPTA1_MOUSE
AccessioniPrimary (citable) accession number: P08032
Secondary accession number(s): B2RWX6, P97502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 7, 2009
Last modified: October 29, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3