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UniProtKB - P07751 (SPTN1_CHICK)

Protein

Spectrin alpha chain, non-erythrocytic 1

Gene

SPTAN1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi2341 – 23521PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi2384 – 23952PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActin capping, Actin-binding, Calmodulin-binding
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain, non-erythrocytic 1
Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Gene namesi
Name:SPTAN1
Synonyms:SPTA2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734541 – 2477Spectrin alpha chain, non-erythrocytic 1Add BLAST2477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1176PhosphotyrosineBy similarity1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1176 – 1177Cleavage; by mu-calpainBy similarity2

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07751
PRIDEiP07751

Interactioni

Subunit structurei

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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

MINTiP07751
STRINGi9031.ENSGALP00000007504

Structurei

Secondary structure

12477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP07751
SMRiP07751
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07751

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati45 – 146Spectrin 1Sequence analysisAdd BLAST102
Repeati150 – 251Spectrin 2Sequence analysisAdd BLAST102
Repeati256 – 358Spectrin 3Sequence analysisAdd BLAST103
Repeati361 – 465Spectrin 4Sequence analysisAdd BLAST105
Repeati468 – 570Spectrin 5Sequence analysisAdd BLAST103
Repeati574 – 676Spectrin 6Sequence analysisAdd BLAST103
Repeati679 – 781Spectrin 7Sequence analysisAdd BLAST103
Repeati785 – 888Spectrin 8Sequence analysisAdd BLAST104
Repeati891 – 969Spectrin 9Sequence analysisAdd BLAST79
Domaini967 – 1026SH3PROSITE-ProRule annotationAdd BLAST60
Repeati1096 – 1162Spectrin 10Sequence analysisAdd BLAST67
Repeati1234 – 1336Spectrin 11Sequence analysisAdd BLAST103
Repeati1339 – 1442Spectrin 12Sequence analysisAdd BLAST104
Repeati1446 – 1549Spectrin 13Sequence analysisAdd BLAST104
Repeati1552 – 1661Spectrin 14Sequence analysisAdd BLAST110
Repeati1664 – 1767Spectrin 15Sequence analysis1 PublicationAdd BLAST104
Repeati1769 – 1873Spectrin 16Sequence analysis3 PublicationsAdd BLAST105
Repeati1876 – 1979Spectrin 17Sequence analysisAdd BLAST104
Repeati1983 – 2086Spectrin 18Sequence analysisAdd BLAST104
Repeati2097 – 2199Spectrin 19Sequence analysisAdd BLAST103
Repeati2211 – 2315Spectrin 20Sequence analysisAdd BLAST105
Domaini2328 – 2363EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini2371 – 2406EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini2409 – 2444EF-hand 3PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 14N-terminal domainAdd BLAST14
Regioni2257 – 2477C-terminal domainAdd BLAST221

Sequence similaritiesi

Belongs to the spectrin family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG0035 Eukaryota
COG5069 LUCA
HOGENOMiHOG000246965
HOVERGENiHBG059266
InParanoidiP07751
KOiK06114
PhylomeDBiP07751

Family and domain databases

CDDicd00051 EFh, 1 hit
cd11808 SH3_Alpha_Spectrin, 1 hit
InterProiView protein in InterPro
IPR035825 Alpha_Spectrin_SH3
IPR011992 EF-hand-dom_pair
IPR014837 EF-hand_Ca_insen
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR018159 Spectrin/alpha-actinin
IPR002017 Spectrin_repeat
PfamiView protein in Pfam
PF13499 EF-hand_7, 1 hit
PF08726 EFhand_Ca_insen, 1 hit
PF00018 SH3_1, 1 hit
PF00435 Spectrin, 20 hits
PRINTSiPR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SM00326 SH3, 1 hit
SM00150 SPEC, 20 hits
SUPFAMiSSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits
PS50002 SH3, 1 hit

Sequencei

Sequence statusi: Complete.

P07751-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSSLRRQKL EDSYRFQFFQ 
        60         70         80         90        100
RDADELGKWI QEKLQIASDE NYKDPSNLQG KLQKHQAFEA EVQANSGAIV 
       110        120        130        140        150
KLDETGNQMI NEGHFASETI RTRLQELHRL WELLLEKMRE KGVKLLQAQK 
       160        170        180        190        200
LVQFLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDLAA 
       210        220        230        240        250
HEERVNEVNQ FAGKLIQEQH PEEELIKSKQ DEVNASWQRL KGLAQQRQGK 
       260        270        280        290        300
LFGAAEVQRF NRDVDETISW IKEKGQLMAS DDFGRDLASV QALLRKHEGL 
       310        320        330        340        350
ERDLAAFHHK VKALCAEADR LQQSHPINAS QIQVKREELI ANWEQIRTLA 
       360        370        380        390        400
AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL 
       410        420        430        440        450
DRHQEHKGEI DAHEDSFRSA DESGQALLAA GHYASDEVKE KLTILSDERS 
       460        470        480        490        500
ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD 
       510        520        530        540        550
SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MDDVATRRDA 
       560        570        580        590        600
LLSRRNALHE RAMKRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 
       610        620        630        640        650
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYASDEVA 
       660        670        680        690        700
ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH 
       710        720        730        740        750
LASDDYGKDL TSVQNLQKKH ALLEADVAAH QDPIDGITIQ ARQFQDAGHF 
       760        770        780        790        800
DADNIKKKQE ALVARYEALK DPMVARKQKL ADSLRLQQLF RDIEDEETWI 
       810        820        830        840        850
REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM 
       860        870        880        890        900
VEEGHFAAED VKIKLNELNQ KWDSLKAKAS QRRQDLEDSL QAQQYFADAN 
       910        920        930        940        950
EAQSWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR 
       960        970        980        990       1000
EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST 
      1010       1020       1030       1040       1050
NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID 
      1060       1070       1080       1090       1100
NQTLITKEVG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA 
      1110       1120       1130       1140       1150
NELQQWINEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI 
      1160       1170       1180       1190       1200
NKVANDLESE GLMAEEVQAV EHQEVYGMMP RDETDSKTVS PWKSARMMVH 
      1210       1220       1230       1240       1250
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SADEVQRFHR DADETKEWIE 
      1260       1270       1280       1290       1300
EKNQALNTDN YGHDLASVQA LQRNDEGFER DLAALGDKVN SLGETAQRLI 
      1310       1320       1330       1340       1350
QSHPELAEDL QEKCTELNQA WSSLGKRADQ RKEKLGDSHD LQRFLSDFRD 
      1360       1370       1380       1390       1400
LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 
      1410       1420       1430       1440       1450
FGQQLLARGH YASPEIKEKL DILDQERTDL EKAWVQRRMM LDQCLELQLF 
      1460       1470       1480       1490       1500
HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 
      1510       1520       1530       1540       1550
IAVLQSFADQ LIAADHYAKG VIANRRNEVL DRWRRLKAQM IEKRSKLGES 
      1560       1570       1580       1590       1600
QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF 
      1610       1620       1630       1640       1650
EAELHANADR IRGVIEMGNP LIERGACAGS EDAVKARLAA LADQWEFLVQ 
      1660       1670       1680       1690       1700
KSSEKSQKLK EANKQQNFNT GIKDFDFWLS EVEALLASED YGKDLASVNN 
      1710       1720       1730       1740       1750
LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV KDKRETINGR 
      1760       1770       1780       1790       1800
FQRIKSMAAA RRAKLNESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD 
      1810       1820       1830       1840       1850
LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGKEEIQQRL 
      1860       1870       1880       1890       1900
AQFVDHWKEL KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS 
      1910       1920       1930       1940       1950
EDYGDTLAAI QGLLKKHEAF ETDFTVHKDR VNDVCANGED LIKKNNHHVE 
      1960       1970       1980       1990       2000
NITAKMKGLK GKVSDLEKAA AQRKAKLDEN SAFLQFNWKA DVVESWIGEK 
      2010       2020       2030       2040       2050
ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN ITALKDQLLA 
      2060       2070       2080       2090       2100
AKHIQSKAIE VRHASLMKRW NQLLANSAAR KKKLLEAQEH FRKVEDLFLT 
      2110       2120       2130       2140       2150
FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA 
      2160       2170       2180       2190       2200
DFNQLAELDR QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK 
      2210       2220       2230       2240       2250
EQRRQEENDK LRQEFAQHAN AFHQWIQETR TYLLDGSCMV EESGTLESQL 
      2260       2270       2280       2290       2300
EATKRKHQEI RAMRSQLKKI EDLGAAMEEA LILDNKYTEH STVGLAQQWD 
      2310       2320       2330       2340       2350
QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF DKDKSGRLNH 
      2360       2370       2380       2390       2400
QEFKSCLRSL GYDLPMVEEG EPDPEFESIL DTVDPNRDGH VSLQEYMAFM 
      2410       2420       2430       2440       2450
ISRETENVKS SEEIESAFRA LSSERKPYVT KEELYQNLTR EQADYCISHM 
      2460       2470 
KPYMDGKGRE LPSAYDYIEF TRSLFVN
Length:2,477
Mass (Da):285,363
Last modified:August 1, 1991 - v3
Checksum:iAD4C876994E6AB39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14518 Genomic DNA Translation: CAA32662.1
X14519 mRNA Translation: CAA32663.1 Sequence problems.
X02593 mRNA Translation: CAB51571.1 Sequence problems.
PIRiA30122 SJCHA
RefSeqiNP_001036003.1, NM_001042538.1
UniGeneiGga.11413

Genome annotation databases

GeneIDi374234
KEGGigga:374234

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14518 Genomic DNA Translation: CAA32662.1
X14519 mRNA Translation: CAA32663.1 Sequence problems.
X02593 mRNA Translation: CAB51571.1 Sequence problems.
PIRiA30122 SJCHA
RefSeqiNP_001036003.1, NM_001042538.1
UniGeneiGga.11413

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray2.02A983-1026[»]
A1030-1090[»]
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[»]
5IHIX-ray1.45A965-1025[»]
5IHKX-ray1.35A965-1025[»]
5IHNX-ray1.50A965-1025[»]
5M6Selectron microscopy4.80A1764-1872[»]
ProteinModelPortaliP07751
SMRiP07751
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiP07751
STRINGi9031.ENSGALP00000007504

Proteomic databases

PaxDbiP07751
PRIDEiP07751

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi374234
KEGGigga:374234

Organism-specific databases

CTDi6709

Phylogenomic databases

eggNOGiKOG0035 Eukaryota
COG5069 LUCA
HOGENOMiHOG000246965
HOVERGENiHBG059266
InParanoidiP07751
KOiK06114
PhylomeDBiP07751

Miscellaneous databases

EvolutionaryTraceiP07751
PROiPR:P07751

Family and domain databases

CDDicd00051 EFh, 1 hit
cd11808 SH3_Alpha_Spectrin, 1 hit
InterProiView protein in InterPro
IPR035825 Alpha_Spectrin_SH3
IPR011992 EF-hand-dom_pair
IPR014837 EF-hand_Ca_insen
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR018159 Spectrin/alpha-actinin
IPR002017 Spectrin_repeat
PfamiView protein in Pfam
PF13499 EF-hand_7, 1 hit
PF08726 EFhand_Ca_insen, 1 hit
PF00018 SH3_1, 1 hit
PF00435 Spectrin, 20 hits
PRINTSiPR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00054 EFh, 2 hits
SM00326 SH3, 1 hit
SM00150 SPEC, 20 hits
SUPFAMiSSF47473 SSF47473, 1 hit
SSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 2 hits
PS50222 EF_HAND_2, 3 hits
PS50002 SH3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSPTN1_CHICK
AccessioniPrimary (citable) accession number: P07751
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1991
Last modified: February 28, 2018
This is version 160 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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