D3ZHV2 · MACF1_RAT
- ProteinMicrotubule-actin cross-linking factor 1
- GeneMacf1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids5430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
F-actin-binding protein which plays a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity).
Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity).
Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity).
Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity).
May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity).
Plays a key role in wound healing and epidermal cell migration (By similarity).
Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity).
Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By similarity).
Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics (By similarity).
Interaction with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers microtubules minus-ends to actin filaments, regulating focal adhesion size and cell migration (By similarity).
May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4 (By similarity).
Plays a key role in wound healing and epidermal cell migration (By similarity).
Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate microtubule dynamics and polarize hair follicle stem cells (By similarity).
As a regulator of actin and microtubule arrangement and stabilization, it plays an essential role in neurite outgrowth, branching and spine formation during brain development (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 5096 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5098 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5100 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5102 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 5107 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 5132 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5134 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5136 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 5138 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 5143 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-actin cross-linking factor 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionD3ZHV2
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity).
Localizes to the tips of microtubules. Associated with the minus-end of microtubules via interaction with CAMSAP3. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (By similarity).
Localizes to the tips of microtubules. Associated with the minus-end of microtubules via interaction with CAMSAP3. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000409709 | 1-5430 | Microtubule-actin cross-linking factor 1 | |||
Sequence: MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQKKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGESGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFPKVPEGGEGISATEVDSRWQEYQSRVDSLIPWIRQHTILMSDKSFPQNPVELKALYNQYIHFKETEILAKEREKGRIKELYKLLEVWIEFGRIKLPQGYHPNHVEEEWGKLIVEMLEREKSLRPAVERLELLLQIANKIQNGALNCEEKLTLAKNTLQADAAHLESGQPVQCESDVIMYIQECEGLIRQLQVDLQILRDEKYYQLEELAFRVMRLQDELVTLRLECTNLYRKGHFTSLELVPPSTLTTTHLKAEPLNKTTHSSSTSWFRKPMTRTELVAISSSEDEGSLRFVYELLSWVEEMQMKLERAEWGNDLPSVELQWETQQHIHTSVEELGSSVKEARLYEGKMSQNFHTSYVETLGKLETQYCKLKETSSFRMRHLQSLHKFVSKATAELIWLNGKEEEELACDWSDSNPNISAKKAYFSELTMELEGKQDVFRSLQDTAELLSLENHPAKQTVEAYSAAVQSQLQWMKQLCLCVEQHIKENAAYFQFFSDARDLESFLRNLQDSIKRKYTCDHNTSLSRLEDLLQDSMDEKEQLIQSKSSVASLVGRSKTIVQLKPRNPDHVLKSTLSVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCLLIPPPNTEAIDVASRVEQSYQKVMALWHQLHINTKSLISWNYLRKDIDAVQTWNLEKLRSSAPGECHQVMKNLQAHYEDFLQDSHDSALFSVADRLRIEEEVEACKTHFQQLMESMENEDKEETLAKVYISELKNIRLRLEECEQRLLKQIQSSASSKTDRDARQDVALRIAEQEHVQEDLKHLRSDLDAVSVKCTTFLQQSPSGSSATTLRSELNLMVEKMDHVYGLSIVCLNKLKTIDVIVRSIQDAELLVKGYEIKLSQEEAVPADLSALESHRTTLQHWLSDVKDKNSVFSVLDEEISKAKAVAEQLHHRAAEPNLDLERYQEKGSQLQERWHRVIAQLETRQSEVESIQEVLRDYRACHGTLIKWIEETTAQQEMMKPGQAEDSRVLSEQLSQQTELFAEIERNQTKLDQCQKLSQQYSTTVKDYELQLMTYKAFVESQQKSPGKRRRMISSSDAITQEFMDLRTRYTALVTLTTQHVKYISDALRRLEEEEKVVEEEKQEHVEKVKDLLGWVSTLARNTQGTTTSSRTSASTDIEKAILEQQVLAEELTTKKEQVSEAIKTSQIFLAKHGHKLSEREKEQISEQLCALNKTYHDLCDGSANQLQQLQSELAQQTEQKTLQKQQDTCHKKLEDLRSWVRQAERALERHRGRASQQELSALQQNQSDLKDLQGDIQNHSTSFATAVKDIEGFLEENQNKLSPQELTALREKLYQAKEQYEGLQDRTREAQKELEEAVTSALQQETEKSKAATELAENRRKIDALLDWVTSVGSSDRQPQTSLPGTEQFSGACLEKQTLDATDGCVDVNQVPEKLDRQYELMKARHQELLSQQQNFIVATQSAQSFLDQHSHNLTPEERQMLQEKLGELKEQYAASLAQSEAKLRQTQTLRDELQKFLQDHREFENWLERSENELDGMHTGGSSPEALNSLLKRQGSFSEDVISHKGDLRFVTISGQKVLETENNFEEGQEPSPTRNLVNEKLKDATERYTTLHSKCTRLGSHLNMLLGQYQQFQSSADSLQAWMLTCEASVEKLLSDTVASDPGILQQQLATTKQLQEELAEHQVPVEKLQKAAHDLMDIEGEPSLDCTPIRETTESIFSRFQSLSCSLAERSALLQKAIAQSQSVQESMESLLQSMKEVEQNLEGEQVAALSSGLIQEALANNMKLKQDIARQKSSLEATREMVTRFMETADGNSAAVLQDRLAELSQRFHRLQLQQQEKESGLKKLLPQAETFEQLSSKLQQFVEHKNRLLASGNQPDQDIAHFSQHIQELTLEMEDQKENLGTLEHLVTALGSCGFALDLSQHQEKIQNLKKDFTELQKTVQEREKDASNCQEQLDEFRKLIRTFQKWLKETEGNVPPAETFVSAKELEKQIEHLKGLLDDWAGKGVLVEEINTKGTALESLIMDITAPDSQAKTGSVLPSVGSSVGSVNGYHTCKDLTEIQCDMSDVNSKYDKLGDALRERQESLQTVLSRMEEVQKEASSVLQWLESKEEVLKGMDASLSPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLEAYPNSQEAENWRKMQEDLNSRWEKATEVTVARQKQLEESASHLACFQAAESQLRPWLMEKELMMGVLGPLSIDPNMLNAQKQQVQFMLKEFEARRQQHEQLTEAAQGILTGPGDVSPSASQVHKDLQSISQKWVELTDKLNSRSTQIDQAIVKSTQYQDLLQDLSEKVKAVGQRLSGQSAISTQPDAVKQQLEETSEIRSDLGQLDDEMKEAQTLCQELSLLIGEQYLKDELKKRLETVALPLQGLEDLAADRMNRLQAALASTQQFQQMFDELRTWLDEKQSQQAKNCPISAKLERLQSQLQENEEFQKNLNQHSGSYEVIVAEGESLLLSVPPGEEKKTLQNQLVELKSHWEDLNKKTVDRQSRLKDCMQKAQKYQWHVEDLVPWIKDCKSKMSELQVTLDPVQLESSLLRSKAMLNEAEKRRSLLEILNSAADILINSSEIDEDEIRDEKAGLNQNMDAITEELQAKTGSLEEMTQRLKEFQESFKNIEKKVEGAKHQLEIFDALGSQACSNKNLEKLKAQREVLQALDPQVDYLRDFTRGLVEDAPDGSDASPLVHQAELAQQEFLEVKQRVNSSCLTMENKLEGIGQFHCRVREMFSQLADLDDELDGMGAIGRDTDSLQSQIEDIRLFLNKIQALRLDIEDSEAECRKMLEEEGTLDLLGLKRELEALNKQCGKLTERGKARQEQLELTLGRVEDFYSKLKALNDAATAAEEGEALQWIVGTEVDVINQQLADFKMFQKEQVDPLQVKLQQVNGLGQGLIQSAGKTCDVQGLEHDMEEVNTRWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLTDTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQAAELADREKITGQLESLECRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIHQQIIRHKALEEEIENHAADVQQAVKIGQSLSSLICPAEQGIMSEKLDSLQARYSEIQDRCCRKASLLEQALFNARLFGEDEVEVLNWLAEVEDKLSAVFVKDYRQDVLQKQHADHLALNEEIINRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFHSTYEELTGWLREVEEELAASGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSHALLELVPWRAREGLDKLVSDANEQYKLVSDTVGQRVDEIDAAIQRSQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRGEIFSTCGEEQKAVLQEKTECLIQQYEAVSLLNSERYARLERAQVLVNQFWETYEELSPWAEETLALIAQLPPPAVDHEQLRQQQEEMRQLRESIAEHKPHIDKILKIGPQLKELNPEEGKMVEEKYQKAENMYAQIKDEVRQRALALDEAVSQSAQIAEFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNKSATMELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFFWEDIKARSEEREIKFLDVLELAEKFWYDMAALLTTIKDTQEIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVKKSIDEMNNAWENLNRTWKERLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIRLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEELMGWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQSTLQQAQGFHSEIEEFLLELNRMESQLSASKPTGGLPETAREQLDAHMELHSQLRAKEEIYNQLLDKGRLMLLSRGDSGSGSKTEQSVALLEQKWHVVSSKVEERKSKLEEALSLATEFQNSLQEFINWLTLAEQSLNIASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWKKLIDWLEDAESHLDSELEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTLLADDAQKLDNLLGEVRDKWDTVCGKSVERQHKLEEALLFSGQFMDALQALVDWLYKVEPQLAEDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIESSRDDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQALKQAEEFRDTVHMLLEWLSEAEQTLRFRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNAAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELLAWIQWAETTLIQRDQEPIPQNIDRVKALITEHQSFMEEMTRKQPDVDRVTKTYKRKNIEPTHAPFIEKSRSGSRKSLNQPTPPPMPILSQSEAKNPRINQLSARWQQVWLLALERQRKLNDALDRLEELKEFANFDFDVWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALHPNKDAYRPTTDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRARGRTNIELREKFILPEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR | ||||||
Modified residue | 4 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 35 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 57 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1122 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1367 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1860 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2429 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2454 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2769 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2895 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 3368 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 4074 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 4252 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 5009 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 5296 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 5321 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 5334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 5372 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 5375 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on serine residues in the C-terminal tail by GSK3B. Phosphorylation inhibits microtubule-binding and this plays a critical role in bulge stem cell migration and skin wound repair. Wnt-signaling can repress phosphorylation (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Family & Domains
Features
Showing features for region, compositional bias, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-47 | Disordered | ||||
Sequence: MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNL | ||||||
Region | 1-295 | Actin-binding | ||||
Sequence: MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQKKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGESGDMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYD | ||||||
Compositional bias | 8-28 | Basic and acidic residues | ||||
Sequence: TLSERSCRSERSCRSERSYRS | ||||||
Domain | 78-181 | Calponin-homology (CH) 1 | ||||
Sequence: RVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQ | ||||||
Repeat | 148-171 | LRR 1 | ||||
Sequence: QRQVKLVNIRNDDITDGNPKLTLG | ||||||
Domain | 194-298 | Calponin-homology (CH) 2 | ||||
Sequence: MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAEDVDVPSPDEKSVITYVSSIYDAFP | ||||||
Repeat | 240-264 | LRR 2 | ||||
Sequence: LVDMERVQIQSNRENLEQAFEVAER | ||||||
Repeat | 377-399 | LRR 3 | ||||
Sequence: LYKLLEVWIEFGRIKLPQGYHPN | ||||||
Repeat | 441-464 | LRR 4 | ||||
Sequence: LNCEEKLTLAKNTLQADAAHLESG | ||||||
Domain | 868-925 | SH3 | ||||
Sequence: KSTLSVKAICDYRQIEITICKNDECVLEDNSQRTKWKVISPTGNEAMVPSVCLLIPPP | ||||||
Repeat | 1050-1073 | LRR 5 | ||||
Sequence: ISELKNIRLRLEECEQRLLKQIQS | ||||||
Repeat | 1128-1154 | LRR 6 | ||||
Sequence: ATTLRSELNLMVEKMDHVYGLSIVCLN | ||||||
Repeat | 1187-1210 | LRR 7 | ||||
Sequence: PADLSALESHRTTLQHWLSDVKDK | ||||||
Repeat | 1257-1282 | LRR 8 | ||||
Sequence: HRVIAQLETRQSEVESIQEVLRDYRA | ||||||
Repeat | 1579-1602 | LRR 9 | ||||
Sequence: QQELSALQQNQSDLKDLQGDIQNH | ||||||
Repeat | 1629-1653 | LRR 10 | ||||
Sequence: LTALREKLYQAKEQYEGLQDRTREA | ||||||
Repeat | 1816-1891 | Spectrin 1 | ||||
Sequence: ELQKFLQDHREFENWLERSENELDGMHTGGSSPEALNSLLKRQGSFSEDVISHKGDLRFVTISGQKVLETENNFEE | ||||||
Repeat | 1869-1891 | LRR 11 | ||||
Sequence: KGDLRFVTISGQKVLETENNFEE | ||||||
Repeat | 1933-2041 | Spectrin 2 | ||||
Sequence: QYQQFQSSADSLQAWMLTCEASVEKLLSDTVASDPGILQQQLATTKQLQEELAEHQVPVEKLQKAAHDLMDIEGEPSLDCTPIRETTESIFSRFQSLSCSLAERSALLQ | ||||||
Repeat | 2058-2083 | LRR 12 | ||||
Sequence: LQSMKEVEQNLEGEQVAALSSGLIQE | ||||||
Repeat | 2194-2220 | LRR 13 | ||||
Sequence: IQELTLEMEDQKENLGTLEHLVTALGS | ||||||
Repeat | 2399-2507 | Spectrin 3 | ||||
Sequence: RMEEVQKEASSVLQWLESKEEVLKGMDASLSPTKTETVKAQAESNKAFLAELEQNSPKIQKVKEALAGLLEAYPNSQEAENWRKMQEDLNSRWEKATEVTVARQKQLEE | ||||||
Repeat | 2444-2467 | LRR 14 | ||||
Sequence: KAFLAELEQNSPKIQKVKEALAGL | ||||||
Repeat | 2534-2557 | LRR 15 | ||||
Sequence: GVLGPLSIDPNMLNAQKQQVQFML | ||||||
Repeat | 2702-2725 | LRR 16 | ||||
Sequence: KKRLETVALPLQGLEDLAADRMNR | ||||||
Repeat | 2733-2837 | Spectrin 4 | ||||
Sequence: TQQFQQMFDELRTWLDEKQSQQAKNCPISAKLERLQSQLQENEEFQKNLNQHSGSYEVIVAEGESLLLSVPPGEEKKTLQNQLVELKSHWEDLNKKTVDRQSRLK | ||||||
Repeat | 2842-2945 | Spectrin 5 | ||||
Sequence: KAQKYQWHVEDLVPWIKDCKSKMSELQVTLDPVQLESSLLRSKAMLNEAEKRRSLLEILNSAADILINSSEIDEDEIRDEKAGLNQNMDAITEELQAKTGSLEE | ||||||
Repeat | 2984-3009 | LRR 17 | ||||
Sequence: NKNLEKLKAQREVLQALDPQVDYLRD | ||||||
Repeat | 3105-3127 | LRR 18 | ||||
Sequence: NKIQALRLDIEDSEAECRKMLEE | ||||||
Repeat | 3169-3274 | Spectrin 6 | ||||
Sequence: EDFYSKLKALNDAATAAEEGEALQWIVGTEVDVINQQLADFKMFQKEQVDPLQVKLQQVNGLGQGLIQSAGKTCDVQGLEHDMEEVNTRWNTLNKKVAQRIAQLQE | ||||||
Repeat | 3214-3237 | LRR 19 | ||||
Sequence: KEQVDPLQVKLQQVNGLGQGLIQS | ||||||
Repeat | 3281-3383 | Spectrin 7 | ||||
Sequence: KFQDALEPLLSWLTDTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQAAELADREKITGQLESLECRWTELLSKAAARQKQLED | ||||||
Repeat | 3388-3491 | Spectrin 8 | ||||
Sequence: AKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIHQQIIRHKALEEEIENHAADVQQAVKIGQSLSSLICPAEQGIMSEKLDSLQARYSEIQDRCCRKASLLE | ||||||
Repeat | 3714-3818 | Spectrin 9 | ||||
Sequence: RSQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRGEIFSTCGEEQKAVLQEKTECLIQQYEAVSLLNSERYARLE | ||||||
Repeat | 3737-3761 | LRR 20 | ||||
Sequence: MALGPIRLEQDQTTAQLQVQKAFSI | ||||||
Repeat | 3825-3927 | Spectrin 10 | ||||
Sequence: NQFWETYEELSPWAEETLALIAQLPPPAVDHEQLRQQQEEMRQLRESIAEHKPHIDKILKIGPQLKELNPEEGKMVEEKYQKAENMYAQIKDEVRQRALALDE | ||||||
Repeat | 3846-3870 | LRR 21 | ||||
Sequence: AQLPPPAVDHEQLRQQQEEMRQLRE | ||||||
Repeat | 4047-4152 | Spectrin 11 | ||||
Sequence: LAEKFWYDMAALLTTIKDTQEIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVKKSIDEMNNAWENLNRTWKERLEKLED | ||||||
Repeat | 4157-4261 | Spectrin 12 | ||||
Sequence: AVQYQDTLQAMFDWLDNTVIRLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLE | ||||||
Repeat | 4267-4370 | Spectrin 13 | ||||
Sequence: LGQFQHALEELMGWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAGDDASSLRSRLETMNQCWESVLQKTEEREQQLQ | ||||||
Repeat | 4375-4481 | Spectrin 14 | ||||
Sequence: QAQGFHSEIEEFLLELNRMESQLSASKPTGGLPETAREQLDAHMELHSQLRAKEEIYNQLLDKGRLMLLSRGDSGSGSKTEQSVALLEQKWHVVSSKVEERKSKLEE | ||||||
Repeat | 4486-4589 | Spectrin 15 | ||||
Sequence: ATEFQNSLQEFINWLTLAEQSLNIASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLD | ||||||
Repeat | 4538-4561 | LRR 22 | ||||
Sequence: RDQIIELDQTGNQLKFLSQKQDVV | ||||||
Repeat | 4594-4700 | Spectrin 16 | ||||
Sequence: RAKQFHEAWKKLIDWLEDAESHLDSELEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTLLADDAQKLDNLLGEVRDKWDTVCGKSVERQHKLEE | ||||||
Repeat | 4707-4808 | Spectrin 17 | ||||
Sequence: QFMDALQALVDWLYKVEPQLAEDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIESSRDDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQ | ||||||
Repeat | 4812-4916 | Spectrin 18 | ||||
Sequence: QAEEFRDTVHMLLEWLSEAEQTLRFRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNAAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLE | ||||||
Region | 4993-5023 | Disordered | ||||
Sequence: PTHAPFIEKSRSGSRKSLNQPTPPPMPILSQ | ||||||
Domain | 5083-5118 | EF-hand 1 | ||||
Sequence: HKKSRVMDFFRRIDKDQDGKITRQEFIDGILASKFP | ||||||
Domain | 5119-5154 | EF-hand 2 | ||||
Sequence: TTKLEMTAVADIFDRDGDGYIDYYEFVAALHPNKDA | ||||||
Domain | 5159-5231 | GAR | ||||
Sequence: TDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCR | ||||||
Region | 5159-5430 | C-terminal tail | ||||
Sequence: TDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRARGRTNIELREKFILPEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR | ||||||
Region | 5247-5430 | Disordered | ||||
Sequence: PEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR | ||||||
Compositional bias | 5266-5345 | Polar residues | ||||
Sequence: PSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRA | ||||||
Region | 5355-5370 | 4 X 4 AA tandem repeats of [GS]-S-R-[AR] | ||||
Sequence: GSRAGSRAGSRASSRR | ||||||
Compositional bias | 5377-5430 | Polar residues | ||||
Sequence: FDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR |
Domain
The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding.
Sequence similarities
Belongs to the plakin or cytolinker family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length5,430
- Mass (Da)619,600
- Last updated2010-04-20 v1
- ChecksumC15B030F89CD5FBF
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JU82 | A0A0G2JU82_RAT | Macf1 | 5474 | ||
M9MMM9 | M9MMM9_RAT | Macf1 | 5431 | ||
A0A8I6AP57 | A0A8I6AP57_RAT | Macf1 | 7375 | ||
A0A8I6ATL8 | A0A8I6ATL8_RAT | Macf1 | 7417 | ||
A0A0G2K9T4 | A0A0G2K9T4_RAT | Macf1 | 7382 | ||
A0A0G2JWA8 | A0A0G2JWA8_RAT | Macf1 | 7352 | ||
A0A8I6AAP8 | A0A8I6AAP8_RAT | Macf1 | 7425 | ||
A0A8I5ZYF6 | A0A8I5ZYF6_RAT | Macf1 | 7395 | ||
A0A8I5YCC2 | A0A8I5YCC2_RAT | Macf1 | 7416 | ||
A0A8I5ZUE8 | A0A8I5ZUE8_RAT | Macf1 | 7345 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-28 | Basic and acidic residues | ||||
Sequence: TLSERSCRSERSCRSERSYRS | ||||||
Compositional bias | 5266-5345 | Polar residues | ||||
Sequence: PSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVISSTGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRA | ||||||
Compositional bias | 5377-5430 | Polar residues | ||||
Sequence: FDLLETQSACSDTSESSAAGGQGSSRRGLTKPSKIPTMSKKTTTASPRTPCPKR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC114512 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC131172 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |