Spectrin alpha chain, erythrocytic 1

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P08032 (SPTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Spectrin alpha chain, erythrocytic 1

Alternative name(s):
Erythroid alpha-spectrin

Gene names

Name:	Spta1
Synonyms:	Spna1, Spta

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2415 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › cell 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 process	Cell shape
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat SH3 domain
Ligand	Actin-binding Calcium Metal-binding
Molecular function	Actin capping
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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 11920196 PubMed 6841965 PubMed 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_component	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 6234993 PubMed 6841965. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2415

2415

Spectrin alpha chain, erythrocytic 1

PRO_0000073453

Regions

Repeat

18 – 50

Spectrin 1

Repeat

52 – 154

103

Spectrin 2

Repeat

156 – 260

105

Spectrin 3

Repeat

262 – 366

105

Spectrin 4

Repeat

368 – 472

105

Spectrin 5

Repeat

474 – 578

105

Spectrin 6

Repeat

580 – 683

104

Spectrin 7

Repeat

685 – 789

105

Spectrin 8

Repeat

791 – 895

105

Spectrin 9

Repeat

897 – 966

Spectrin 10

Domain

975 – 1034

SH3

Repeat

1080 – 1179

100

Spectrin 11

Repeat

1181 – 1285

105

Spectrin 12

Repeat

1287 – 1391

105

Spectrin 13

Repeat

1393 – 1496

104

Spectrin 14

Repeat

1498 – 1603

106

Spectrin 15

Repeat

1605 – 1709

105

Spectrin 16

Repeat

1711 – 1815

105

Spectrin 17

Repeat

1817 – 1922

106

Spectrin 18

Repeat

1924 – 2029

106

Spectrin 19

Repeat

2039 – 2143

105

Spectrin 20

Repeat

2153 – 2254

102

Spectrin 21

Domain

2267 – 2302

EF-hand 1

Domain

2310 – 2345

EF-hand 2

Domain

2347 – 2382

EF-hand 3

Calcium binding

2280 – 2291

1 Potential

Calcium binding

2323 – 2334

2 Potential

Experimental info

Sequence conflict

337

P → L in AAB47540. Ref.1

Sequence conflict

501

D → Y in AAI50748. Ref.4

Sequence conflict

716

G → V in AAB47540. Ref.1

Sequence conflict

741

V → M in AAB47540. Ref.1

Sequence conflict

741

V → M in AAI50748. Ref.4

Sequence conflict

1044 – 1045

RQ → QR in AAB47540. Ref.1

Sequence conflict

1044 – 1045

RQ → QR in AAI50748. Ref.4

Sequence conflict

1225

V → C in AAB47540. Ref.1

Sequence conflict

1238

T → N in AAB47540. Ref.1

Sequence conflict

1425

N → D in AAB47540. Ref.1

Sequence conflict

1582

K → M in AAB47540. Ref.1

Sequence conflict

2062

L → M in AAB47540. Ref.1

Sequence conflict

2062

L → M in AAI50748. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P08032 [UniParc].

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

FASTA

2,415

279,865

        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' referencesShow '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. 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.
IPI	IPI00323230.
PIR	A05283.
RefSeq	NP_035595.2. NM_011465.4.
UniGene	Mm.200611.
3D structure databases
ProteinModelPortal	P08032.
SMR	P08032. Positions 4-953, 992-1032, 1047-2260, 2272-2373.
ModBase	Search...
PTM databases
PhosphoSite	P08032.
Proteomic databases
PaxDb	P08032.
PRIDE	P08032.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027817; ENSMUSP00000027817; ENSMUSG00000026532.
GeneID	20739.
KEGG	mmu:20739.
UCSC	uc007dsw.2. mouse.
Organism-specific databases
CTD	6708.
MGI	MGI:98385. Spta1.
Phylogenomic databases
eggNOG	NOG237318.
GeneTree	ENSGT00700000104022.
HOGENOM	HOG000246965.
HOVERGEN	HBG059266.
InParanoid	B2RWX6.
KO	K06114.
OMA	EFWLSEA.
OrthoDB	EOG4PC9R6.
Gene expression databases
Bgee	P08032.
CleanEx	MM_SPNA1.
Genevestigator	P08032.
GermOnline	ENSMUSG00000026532. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 2 hits.
InterPro	IPR011992. EF-hand-like_dom. 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]
Pfam	PF08726. efhand_Ca_insen. 1 hit. PF00018. SH3_1. 1 hit. PF00435. Spectrin. 20 hits. [Graphical view]
PRINTS	PR01887. SPECTRNALPHA.
SMART	SM00326. SH3. 1 hit. SM00150. SPEC. 20 hits. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS50222. EF_HAND_2. 3 hits. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299373.
SOURCE	Search...

Entry information

Entry name

SPTA1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents