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P07751 (SPTN1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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, non-erythrocytic 1
Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Gene names
Name:SPTAN1
Synonyms:SPTA2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length2477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.

Subunit structure

Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts with ACP1 By similarity.

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex.

Domain

Spectrin-like proteins have five domains: (1) N-terminal domain (N), (2) domain between the N-terminal and middle domain (NM), (3) middle domain (M), (4) domain between the middle and C-terminal domain (MC), (5) C-terminal domain (C). NM and MC domains are composed of typical spectrin 106 residues repeats (1-8 for NM and 12-19 for MC) and are homologous to each other. N, M, and C domains are composed of sequences that do not form typical spectrin repeats.

Post-translational modification

Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro By similarity.

Sequence similarities

Belongs to the spectrin family.

Contains 3 EF-hand domains.

Contains 1 SH3 domain.

Contains 20 spectrin repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DomainRepeat
SH3 domain
   LigandActin-binding
Calcium
Calmodulin-binding
Metal-binding
   Molecular functionActin capping
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24772477Spectrin alpha chain, non-erythrocytic 1
PRO_0000073454

Regions

Repeat15 – 119105Spectrin 1
Repeat120 – 225106Spectrin 2
Repeat226 – 331106Spectrin 3
Repeat332 – 437106Spectrin 4
Repeat438 – 543106Spectrin 5
Repeat544 – 648105Spectrin 6
Repeat649 – 754106Spectrin 7
Repeat755 – 860106Spectrin 8
Repeat861 – 966106Spectrin 9
Domain967 – 102660SH3
Repeat1062 – 1167106Spectrin 10
Repeat1204 – 1309106Spectrin 11
Repeat1310 – 1415106Spectrin 12
Repeat1416 – 1521106Spectrin 13
Repeat1522 – 1633112Spectrin 14
Repeat1634 – 1739106Spectrin 15
Repeat1740 – 1845106Spectrin 16
Repeat1846 – 1951106Spectrin 17
Repeat1952 – 2058107Spectrin 18
Repeat2059 – 2171113Spectrin 19
Repeat2172 – 225685Spectrin 20
Domain2328 – 236336EF-hand 1
Domain2371 – 240636EF-hand 2
Domain2409 – 244436EF-hand 3
Calcium binding2341 – 2352121 Potential
Calcium binding2384 – 2395122 Potential
Region1 – 1414N-terminal domain
Region2257 – 2477221C-terminal domain

Sites

Site1176 – 11772Cleavage; by mu-calpain By similarity

Amino acid modifications

Modified residue11761Phosphotyrosine By similarity

Secondary structure

................................. 2477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07751 [UniParc].

Last modified August 1, 1991. Version 3.
Checksum: AD4C876994E6AB39

FASTA2,477285,363
        10         20         30         40         50         60 
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ RDADELGKWI 

        70         80         90        100        110        120 
QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV KLDETGNQMI NEGHFASETI 

       130        140        150        160        170        180 
RTRLQELHRL WELLLEKMRE KGVKLLQAQK LVQFLRECED VMDWINDKEA IVTSEELGQD 

       190        200        210        220        230        240 
LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNASWQRL 

       250        260        270        280        290        300 
KGLAQQRQGK LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL 

       310        320        330        340        350        360 
ERDLAAFHHK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA AERHARLNDS 

       370        380        390        400        410        420 
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFRSA 

       430        440        450        460        470        480 
DESGQALLAA GHYASDEVKE KLTILSDERS ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 

       490        500        510        520        530        540 
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 

       550        560        570        580        590        600 
MDDVATRRDA LLSRRNALHE RAMKRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 

       610        620        630        640        650        660 
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA ARMNEVISLW 

       670        680        690        700        710        720 
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TSVQNLQKKH 

       730        740        750        760        770        780 
ALLEADVAAH QDPIDGITIQ ARQFQDAGHF DADNIKKKQE ALVARYEALK DPMVARKQKL 

       790        800        810        820        830        840 
ADSLRLQQLF RDIEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 

       850        860        870        880        890        900 
KAVTQKGNAM VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN 

       910        920        930        940        950        960 
EAQSWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 

       970        980        990       1000       1010       1020 
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 

      1030       1040       1050       1060       1070       1080 
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTLITKEVG SVSLRMKQVE ELYHSLLELG 

      1090       1100       1110       1120       1130       1140 
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL 

      1150       1160       1170       1180       1190       1200 
KANESRLKDI NKVANDLESE GLMAEEVQAV EHQEVYGMMP RDETDSKTVS PWKSARMMVH 

      1210       1220       1230       1240       1250       1260 
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SADEVQRFHR DADETKEWIE EKNQALNTDN 

      1270       1280       1290       1300       1310       1320 
YGHDLASVQA LQRNDEGFER DLAALGDKVN SLGETAQRLI QSHPELAEDL QEKCTELNQA 

      1330       1340       1350       1360       1370       1380 
WSSLGKRADQ RKEKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 

      1390       1400       1410       1420       1430       1440 
HQEHRTEIDA RAGTFQAFEQ FGQQLLARGH YASPEIKEKL DILDQERTDL EKAWVQRRMM 

      1450       1460       1470       1480       1490       1500 
LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 

      1510       1520       1530       1540       1550       1560 
IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 

      1570       1580       1590       1600       1610       1620 
DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIEMGNP 

      1630       1640       1650       1660       1670       1680 
LIERGACAGS EDAVKARLAA LADQWEFLVQ KSSEKSQKLK EANKQQNFNT GIKDFDFWLS 

      1690       1700       1710       1720       1730       1740 
EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV 

      1750       1760       1770       1780       1790       1800 
KDKRETINGR FQRIKSMAAA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD 

      1810       1820       1830       1840       1850       1860 
LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL AQFVDHWKEL 

      1870       1880       1890       1900       1910       1920 
KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF 

      1930       1940       1950       1960       1970       1980 
ETDFTVHKDR VNDVCANGED LIKKNNHHVE NITAKMKGLK GKVSDLEKAA AQRKAKLDEN 

      1990       2000       2010       2020       2030       2040 
SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN 

      2050       2060       2070       2080       2090       2100 
ITALKDQLLA AKHIQSKAIE VRHASLMKRW NQLLANSAAR KKKLLEAQEH FRKVEDLFLT 

      2110       2120       2130       2140       2150       2160 
FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR 

      2170       2180       2190       2200       2210       2220 
QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN 

      2230       2240       2250       2260       2270       2280 
AFHQWIQETR TYLLDGSCMV EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA 

      2290       2300       2310       2320       2330       2340 
LILDNKYTEH STVGLAQQWD QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF 

      2350       2360       2370       2380       2390       2400 
DKDKSGRLNH QEFKSCLRSL GYDLPMVEEG EPDPEFESIL DTVDPNRDGH VSLQEYMAFM 

      2410       2420       2430       2440       2450       2460 
ISRETENVKS SEEIESAFRA LSSERKPYVT KEELYQNLTR EQADYCISHM KPYMDGKGRE 

      2470 
LPSAYDYIEF TRSLFVN 

« Hide

References

[1]"Primary structure of the brain alpha-spectrin."
Wasenius V.-M., Saraste M., Salven P., Eraemaa M., Holm L., Lehto V.-P.
J. Cell Biol. 108:79-93(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]Erratum
Wasenius V.-M., Saraste M., Salven P., Eraemaa M., Holm L., Lehto V.-P.
J. Cell Biol. 108:1177-1178(1989)
Cited for: SEQUENCE REVISION.
[3]"Sequencing of the chicken non-erythroid spectrin cDNA reveals an internal repetitive structure homologous to the human erythrocyte spectrin."
Wasenius V.-M., Saraste M., Knowles J., Virtanen I., Lehto V.-P.
EMBO J. 4:1425-1430(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1695-2153.
[4]"Crystal structure of a Src-homology 3 (SH3) domain."
Musacchio A., Noble M., Pauptit R., Wierenga R.K., Saraste M.
Nature 359:851-855(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 965-1025.
[5]"Obligatory steps in protein folding and the conformational diversity of the transition state."
Martinez J.C., Pisabarro M.T., Serrano L.
Nat. Struct. Biol. 5:721-729(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 969-1025.
[6]"Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil."
Pascual J., Pfuhl M., Walther D., Saraste M., Nilges M.
J. Mol. Biol. 273:740-751(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1763-1872.
[7]"Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands."
Trave G., Lacombe J.-P., Pfuhl M., Saraste M., Pastore A.
EMBO J. 14:4922-4931(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2320-2403.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14518 Genomic DNA. Translation: CAA32662.1.
X14519 mRNA. Translation: CAA32663.1. Sequence problems.
X02593 mRNA. Translation: CAB51571.1. Sequence problems.
PIRSJCHA. A30122.
RefSeqNP_001036003.1. NM_001042538.1.
UniGeneGga.11413.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AEYNMR-A965-1025[»]
1AJ3NMR-A1763-1872[»]
1BK2X-ray2.01A969-1025[»]
1CUNX-ray2.00A/B/C1770-1982[»]
1E6GX-ray2.30A965-1025[»]
1E6HX-ray2.01A965-1025[»]
1E7OX-ray3.20A965-1025[»]
1G2BX-ray1.12A967-1025[»]
1H8KX-ray2.70A965-1025[»]
1HD3X-ray1.98A965-1025[»]
1M8MNMR-A965-1025[»]
1NEGX-ray2.30A965-1024[»]
1PWTX-ray1.77A967-1025[»]
1QKWX-ray2.00A964-1025[»]
1QKXX-ray1.80A964-1025[»]
1SHGX-ray1.80A965-1025[»]
1TUCX-ray2.02A967-1025[»]
1TUDX-ray1.77A964-1010[»]
1U06X-ray1.49A965-1025[»]
1U4QX-ray2.50A/B1662-1982[»]
1U5PX-ray2.00A1662-1876[»]
1UUEX-ray2.60A965-1025[»]
2CDTX-ray2.54A965-1025[»]
2F2VX-ray1.85A965-1025[»]
2F2WX-ray1.70A965-1025[»]
2F2XX-ray1.60A965-1025[»]
2JM8NMR-A965-1025[»]
2JM9NMR-A965-1025[»]
2JMANMR-A965-1025[»]
2JMCNMR-A983-1025[»]
2KR3NMR-A965-1025[»]
2KXDNMR-A967-1025[»]
2LJ3NMR-A965-1025[»]
2NUZX-ray1.85A965-1025[»]
2OAWX-ray1.90A/B/C/D969-1025[»]
2RMONMR-A965-1025[»]
2ROTNMR-A965-1025[»]
3I9QX-ray1.45A969-1025[»]
3M0PX-ray2.60A965-1025[»]
3M0QX-ray1.75A965-1025[»]
3M0RX-ray1.10A965-1025[»]
3M0SX-ray1.60A969-1025[»]
3M0TX-ray1.70A965-1025[»]
3M0UX-ray1.10A965-1025[»]
3NGPX-ray1.08A965-1025[»]
4F16X-ray1.93A965-1025[»]
4F17X-ray1.55A965-1025[»]
ProteinModelPortalP07751.
SMRP07751. Positions 1-147, 967-1025, 1443-1549, 1662-1979.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-139133.
STRING9031.ENSGALP00000007504.

Proteomic databases

PaxDbP07751.
PRIDEP07751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374234.
KEGGgga:374234.

Organism-specific databases

CTD6709.

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000246965.
HOVERGENHBG059266.
KOK06114.
PhylomeDBP07751.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07751.
NextBio20813733.
PROP07751.

Entry information

Entry nameSPTN1_CHICK
AccessionPrimary (citable) accession number: P07751
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 138 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references