| Tag |
Content |
| dbPAF ID |
dbPAF-0005741 |
| Uniprot Accession |
P13395; SPTCA_DROME; Q26340; Q3KN50; Q8SZW7; Q9W085;
|
| Genbank Protein ID |
NP_476739.1;
|
| Genbank Nucleotide ID |
NM_057391.4;
|
| Protein Name |
Spectrin alpha chain |
| Protein Synonyms/Alias |
|
| Gene Name |
alpha-Spec |
| Gene Synonyms/Alias |
SPEC-A;CG1977; |
| Organism |
Drosophila melanogaster(Fruit fly) |
| NCBI Taxa ID |
7227 |
Functional Description
(View all) |
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. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization.Functional Description
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. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. |
Phosphorylation Sites
|
dbPAF PTMs: 10 |
Sequence
(Fasta) | MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ YFKRDADELE 60
SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN AIVSLDNTGQ EMINQQHFAS 120
ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ ALVLVQFLRQ CEEVMFWIKD KETFVTADEF 180
GQDLEHVEVL QRKFDEFQKD MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW 240
QRLKQLAIVR QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH 300
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT TKARERKQKL 360
DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE ALLERHQEHK GEIDAREDSF 420
KLTTESGQKL LEREHYAAAE IQEKLAALEN DKSSLLSLWE DRRILYEQCM DLQLFYRDTE 480
QADTWMAKQE AFLANEDLGD SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ 540
HYAADDVAQR RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT 600
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD QINTRMQEIV 660
VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI EGQLLSEDHG KDLTSVQNLQ 720
KKHALLEADV MAHQDRIESI KVAANKFIES GHFDADNIRN KEGNLSARYA ALAAPMGERK 780
QHLLDSLQVQ QLFRDLEDEA AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE 840
ARLLNVISSG ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA 900
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ ALQEQAKNCR 960
QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL NSNNKDWWKV EVNDRQGFVP 1020
AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ INSQYDNLLA LARERQNKLN ETVKAYVLVR 1080
EAADLAQWIR DKENHAQIAD VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL 1140
TSLGQTEAAL KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK 1200
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS HPDTAEQTYA 1260
KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL AWINSMMSLV TSDELANDVT 1320
GAEALIERHQ EHRTEIDARA GTFGAFEQFG NELLQANHYA SPEIKEKIED LAKAREDLEK 1380
AWTERRLQLE QNLDLQLYMR DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK 1440
AINGHEQKIA ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT 1500
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN ADRIQSVLAM 1560
GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL KLKEANKQRT YIAAVKDLDF 1620
WLGEVESLLT TEDSGKDLAS VQNLMKKHQL VEADIVAHED RIKDMNNQAD SLVESGQFDT 1680
AGIQEKRQSI NERYERICNL AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY 1740
GRDLTGVQNL KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW 1800
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM AAVQGLLKKH 1860
DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ QLRLKLDNLS ALAARRKGAL 1920
LDNSAYLQFM WKADVVESWI DDKENYVRSD EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG 1980
IHNITALKDQ LINASHAQSP AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL 2040
YLTFAKKASA FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA 2100
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE NDKLRKEFAK 2160
HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR RVDLKKIEEL GALLEEHLIL 2220
DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL EQQIQARNHS GVSEDSLKEF SMMFKHFDKD 2280
KSGKLNHQEF KSCLRALGYD LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK 2340
ETENVQSYEE IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK 2400
DALDYIDFTR TLFQN
2416Fasta Sequence
>P13395|alpha-Spec|Drosophila melanogaster(Fruit fly)
MENFTPKEVKILETVEDIQERREQVLSRYNDFKIETRQKREKLEDSRRFQYFKRDADELESWIHEKLQAASEESYRDPTNLQAKIQKHQAFEAEVSAHSNAIVSLDNTGQEMINQQHFASESIQVRLDELHKLWELLLSRLAEKGLKLQQALVLVQFLRQCEEVMFWIKDKETFVTADEFGQDLEHVEVLQRKFDEFQKDMASQEYRVTEVNQLADKLVQDGHPERDTITKRKEELNEAWQRLKQLAIVRQEKLFGAHEIQRFNRDADETVAWIAEKDVVLSSDDYGRDLASVQALQRKHEGVERDLAALEDKVSTLGAEAQRLCSIHADHSDQIRDKQAEIANYWQSLTTKARERKQKLDESYYLHRFLADFRDLVSWINGMKAIISADELAKDVAGAEALLERHQEHKGEIDAREDSFKLTTESGQKLLEREHYAAAEIQEKLAALENDKSSLLSLWEDRRILYEQCMDLQLFYRDTEQADTWMAKQEAFLANEDLGDSLDSVEALIKKHEDFEKSLAAQEEKIKALDIFATKLIDGQHYAADDVAQRRQMLLARRAALQEKSSKRRQLLEDSNRYQQFERDCDETKGWISEKLKFATDDSYLDPTNLNGKMQKHQNFEHELNANKSRIEDITNVGTELIEKQHYAADQINTRMQEIVVLWETLVQASDKKGTKLNEACQQQQFNRTIEDIELWLSEIEGQLLSEDHGKDLTSVQNLQKKHALLEADVMAHQDRIESIKVAANKFIESGHFDADNIRNKEGNLSARYAALAAPMGERKQHLLDSLQVQQLFRDLEDEAAWIREKEPIAASTNRGRDLIGVQNLIKKHQAVLAEINNHEARLLNVISSGENMLKDQPFASDDIRQRLEALQEQWNTLKEKSSQRKQDLDDSLQAHQYFADANEAESWMREKEPIATGSDYGKDEDSSEALLKKHEALVSDLEAFGNTIQALQEQAKNCRQQETPVVDITGKECVVALYDYTEKSPREVSMKKGDVLTLLNSNNKDWWKVEVNDRQGFVPAAYIKKIDAGLSASQQNLVDNHSIAKRQNQINSQYDNLLALARERQNKLNETVKAYVLVREAADLAQWIRDKENHAQIADVVGEDLEEVEVLQKKFDDFNDDLKANEVRLANMNEIAVQLTSLGQTEAALKIQTQMQDLNEKWNNLQTLTAEKASQLGSAHEVQRFHRDIDETKDWIAEKANALNNDDLGKDLRSVQTLQRKHEGVERDLAALRDKIRQLDETANRLMQSHPDTAEQTYAKQKEINEMWDQIITKSTARKEKLLDSYDLQRFLSDYRDLLAWINSMMSLVTSDELANDVTGAEALIERHQEHRTEIDARAGTFGAFEQFGNELLQANHYASPEIKEKIEDLAKAREDLEKAWTERRLQLEQNLDLQLYMRDCELAESWMSAREAFLNADDDANAGGNVEALIKKHEDFDKAINGHEQKIAALQTVADQLIAQNHYASNLVDEKRKQVLERWRHLKEGLIEKRSRLGDEQTLQQFSRDADEIENWIAEKLQLATEESYKDPANIQSKHQKHQAFEAELAANADRIQSVLAMGGNLIDKKQCSGSEDAVQKRLTQIADQWEYLTHKTTEKSLKLKEANKQRTYIAAVKDLDFWLGEVESLLTTEDSGKDLASVQNLMKKHQLVEADIVAHEDRIKDMNNQADSLVESGQFDTAGIQEKRQSINERYERICNLAAHRQARLNEALTLHQFFRDIADEESWIKEKKLLVGSDDYGRDLTGVQNLKKKHKRLEAELGSHEPAIQAVQEAGEKLMDVSNLGVPEIEQRLKALNQAWAELKNLAATRGQKLDESLTYQQFLAQVEEEEAWITEKQQLLSVEDYGDSMAAVQGLLKKHDAFETDFTAHKDRCSLICDQGSELVEAKNHHGESIAQRCQQLRLKLDNLSALAARRKGALLDNSAYLQFMWKADVVESWIDDKENYVRSDEFGRDLSTVQTLLTKQETFDAGLNAFEQEGIHNITALKDQLINASHAQSPAILKRHGDVIARWQKLRDASNTRKDRLLAMQEQFRQIEELYLTFAKKASAFNSWFENAEEDLTDPVRCNSIEEIRALRDAHAQFQASLSSAEADFKALAALDQKIKSFNVGPNPYTWFTMEALEETWRNLQKIIEERDGELAKEAKRQEENDKLRKEFAKHANLFHQWLTETRTSMMEGSGSLEQQLEALRVKATEVRARRVDLKKIEELGALLEEHLILDNRYTEHSTVGLAQQWDQLDQLSMRMQHNLEQQIQARNHSGVSEDSLKEFSMMFKHFDKDKSGKLNHQEFKSCLRALGYDLPMVEEGQPDPEFEAILDVVDPNRDGYVSLQEYIAFMISKETENVQSYEEIENAFRAITAADRPYVTKEELYCNLTKDMADYCVQRMKPFSEPRSGQPIKDALDYIDFTRTLFQN
|
| Keyword |
KW-0002--3D-structure
KW-0117--Actin capping
KW-0009--Actin-binding
KW-0106--Calcium
KW-0112--Calmodulin-binding
KW-0133--Cell shape
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0206--Cytoskeleton
KW-0333--Golgi apparatus
KW-0479--Metal-binding
KW-0597--Phosphoprotein
KW-1185--Reference proteome
KW-0677--Repeat
KW-0728--SH3 domain
|
| Interpro |
IPR011992--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
|
| PROSITE |
PS00018--EF_HAND_1
PS50222--EF_HAND_2
PS50002--SH3
|
| Pfam |
PF13499--EF-hand_7
PF08726--EFhand_Ca_insen
PF00018--SH3_1
PF00435--Spectrin
|
| Gene Ontology |
GO:0016323--C:basolateral plasma membrane
GO:0005938--C:cell cortex
GO:0045169--C:fusome
GO:0005794--C:Golgi apparatus
GO:0005811--C:lipid particle
GO:0031594--C:neuromuscular junction
GO:0005886--C:plasma membrane
GO:0008091--C:spectrin
GO:0045170--C:spectrosome
GO:0003779--F:actin binding
GO:0005509--F:calcium ion binding
GO:0008092--F:cytoskeletal protein binding
GO:0008017--F:microtubule binding
GO:0051693--P:actin filament capping
GO:0016199--P:axon midline choice point recognition
GO:0007417--P:central nervous system development
GO:0060429--P:epithelium development
GO:0045478--P:fusome organization
GO:0048134--P:germ-line cyst formation
GO:0007293--P:germarium-derived egg chamber formation
GO:0030727--P:germarium-derived female germ-line cyst formation
GO:0007294--P:germarium-derived oocyte fate determination
GO:0042062--P:long-term strengthening of neuromuscular junction
GO:0048790--P:maintenance of presynaptic active zone structure
GO:0007026--P:negative regulation of microtubule depolymerization
GO:0007274--P:neuromuscular synaptic transmission
GO:0007308--P:oocyte construction
GO:0030707--P:ovarian follicle cell development
GO:0007009--P:plasma membrane organization
GO:0008360--P:regulation of cell shape
GO:0050807--P:regulation of synapse organization
GO:0030721--P:spectrosome organization
|
