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Protein

Microtubule-actin cross-linking factor 1

Gene

Macf1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

F-actin-binding protein which may play 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. 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. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi5096 – 5107121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi5132 – 5143122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-actin cross-linking factor 1
Alternative name(s):
Actin cross-linking family 7
Gene namesi
Name:Macf1
Synonyms:Acf7, Aclp7, Macf
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306057. Macf1.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cytoplasm By similarity
  • Membrane 1 Publication
  • Cell membrane By similarity
  • Cell projectionruffle membrane By similarity

  • Note: Localizes to the tips of microtubules. APC controls its localization to the cell membrane which is critical for its function in microtubule stabilization. The phosphorylated form is found in the cytoplasm while the non-phosphorylated form associates with the microtubules (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 54305430Microtubule-actin cross-linking factor 1PRO_0000409709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineCombined sources
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei280 – 2801PhosphoserineCombined sources
Modified residuei1122 – 11221PhosphoserineBy similarity
Modified residuei1367 – 13671PhosphoserineBy similarity
Modified residuei1376 – 13761PhosphoserineBy similarity
Modified residuei1860 – 18601PhosphoserineCombined sources
Modified residuei2429 – 24291PhosphoserineCombined sources
Modified residuei2454 – 24541PhosphoserineCombined sources
Modified residuei2769 – 27691PhosphoserineBy similarity
Modified residuei2895 – 28951PhosphoserineBy similarity
Modified residuei3368 – 33681PhosphothreonineBy similarity
Modified residuei4074 – 40741PhosphoserineCombined sources
Modified residuei4252 – 42521N6-acetyllysineBy similarity
Modified residuei5009 – 50091PhosphoserineBy similarity
Modified residuei5296 – 52961PhosphothreonineCombined sources
Modified residuei5321 – 53211PhosphoserineBy similarity
Modified residuei5334 – 53341PhosphoserineBy similarity
Modified residuei5372 – 53721PhosphoserineBy similarity
Modified residuei5375 – 53751PhosphoserineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiD3ZHV2.
PeptideAtlasiD3ZHV2.

PTM databases

iPTMnetiD3ZHV2.

Interactioni

Subunit structurei

Interacts with MAPRE1, CLASP1, CLASP2 and GOLGA4 (By similarity). Interacts with AXIN1 and LRP6. Found in a complex composed of MACF1, APC; AXIN1, CTNNB1 and GSK3B.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041065.

Structurei

3D structure databases

ProteinModelPortaliD3ZHV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 295295Actin-bindingAdd
BLAST
Domaini78 – 181104CH 1PROSITE-ProRule annotationAdd
BLAST
Repeati148 – 17124LRR 1Add
BLAST
Domaini194 – 295102CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati240 – 26425LRR 2Add
BLAST
Repeati377 – 39923LRR 3Add
BLAST
Repeati441 – 46424LRR 4Add
BLAST
Domaini871 – 92353SH3Add
BLAST
Repeati1050 – 107324LRR 5Add
BLAST
Repeati1128 – 115427LRR 6Add
BLAST
Repeati1187 – 121024LRR 7Add
BLAST
Repeati1257 – 128226LRR 8Add
BLAST
Repeati1579 – 160224LRR 9Add
BLAST
Repeati1629 – 165325LRR 10Add
BLAST
Repeati1816 – 189176Spectrin 1Add
BLAST
Repeati1869 – 189123LRR 11Add
BLAST
Repeati1933 – 2041109Spectrin 2Add
BLAST
Repeati2058 – 208326LRR 12Add
BLAST
Repeati2194 – 222027LRR 13Add
BLAST
Repeati2399 – 2507109Spectrin 3Add
BLAST
Repeati2444 – 246724LRR 14Add
BLAST
Repeati2534 – 255724LRR 15Add
BLAST
Repeati2702 – 272524LRR 16Add
BLAST
Repeati2733 – 2837105Spectrin 4Add
BLAST
Repeati2842 – 2945104Spectrin 5Add
BLAST
Repeati2984 – 300926LRR 17Add
BLAST
Repeati3105 – 312723LRR 18Add
BLAST
Repeati3169 – 3274106Spectrin 6Add
BLAST
Repeati3214 – 323724LRR 19Add
BLAST
Repeati3281 – 3383103Spectrin 7Add
BLAST
Repeati3388 – 3491104Spectrin 8Add
BLAST
Repeati3714 – 3818105Spectrin 9Add
BLAST
Repeati3737 – 376125LRR 20Add
BLAST
Repeati3825 – 3927103Spectrin 10Add
BLAST
Repeati3846 – 387025LRR 21Add
BLAST
Repeati4047 – 4152106Spectrin 11Add
BLAST
Repeati4157 – 4261105Spectrin 12Add
BLAST
Repeati4267 – 4370104Spectrin 13Add
BLAST
Repeati4375 – 4481107Spectrin 14Add
BLAST
Repeati4486 – 4589104Spectrin 15Add
BLAST
Repeati4538 – 456124LRR 22Add
BLAST
Repeati4594 – 4700107Spectrin 16Add
BLAST
Repeati4707 – 4808102Spectrin 17Add
BLAST
Repeati4812 – 4916105Spectrin 18Add
BLAST
Domaini5083 – 511836EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini5119 – 515436EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini5159 – 523173GARPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5159 – 5430272C-terminal tailBy similarityAdd
BLAST
Regioni5355 – 5370164 X 4 AA tandem repeats of [GS]-S-R-[AR]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi700 – 7034Poly-Glu
Compositional biasi1414 – 14174Poly-Glu
Compositional biasi5264 – 5401138Ser-richAdd
BLAST

Domaini

The C-terminal tail is required for phosphorylation by GSK3B and for microtubule-binding.By similarity

Sequence similaritiesi

Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 GAR domain.PROSITE-ProRule annotation
Contains 22 LRR (leucine-rich) repeats.Curated
Contains 1 SH3 domain.Curated
Contains 18 spectrin repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
COG5069. LUCA.
InParanoidiD3ZHV2.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS_dom.
IPR028408. Macf1.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF37. PTHR11915:SF37. 5 hits.
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00150. SPEC. 34 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZHV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH
60 70 80 90 100
EQKKRKSQDS VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN
110 120 130 140 150
DLYEDLRDGH NLISLLEVLS GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ
160 170 180 190 200
VKLVNIRNDD ITDGNPKLTL GLIWTIILHF QISDIYISGE SGDMSAKEKL
210 220 230 240 250
LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL VDMERVQIQS
260 270 280 290 300
NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV
310 320 330 340 350
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI RQHTILMSDK SFPQNPVELK
360 370 380 390 400
ALYNQYIHFK ETEILAKERE KGRIKELYKL LEVWIEFGRI KLPQGYHPNH
410 420 430 440 450
VEEEWGKLIV EMLEREKSLR PAVERLELLL QIANKIQNGA LNCEEKLTLA
460 470 480 490 500
KNTLQADAAH LESGQPVQCE SDVIMYIQEC EGLIRQLQVD LQILRDEKYY
510 520 530 540 550
QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP STLTTTHLKA
560 570 580 590 600
EPLNKTTHSS STSWFRKPMT RTELVAISSS EDEGSLRFVY ELLSWVEEMQ
610 620 630 640 650
MKLERAEWGN DLPSVELQWE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF
660 670 680 690 700
HTSYVETLGK LETQYCKLKE TSSFRMRHLQ SLHKFVSKAT AELIWLNGKE
710 720 730 740 750
EEELACDWSD SNPNISAKKA YFSELTMELE GKQDVFRSLQ DTAELLSLEN
760 770 780 790 800
HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ HIKENAAYFQ FFSDARDLES
810 820 830 840 850
FLRNLQDSIK RKYTCDHNTS LSRLEDLLQD SMDEKEQLIQ SKSSVASLVG
860 870 880 890 900
RSKTIVQLKP RNPDHVLKST LSVKAICDYR QIEITICKND ECVLEDNSQR
910 920 930 940 950
TKWKVISPTG NEAMVPSVCL LIPPPNTEAI DVASRVEQSY QKVMALWHQL
960 970 980 990 1000
HINTKSLISW NYLRKDIDAV QTWNLEKLRS SAPGECHQVM KNLQAHYEDF
1010 1020 1030 1040 1050
LQDSHDSALF SVADRLRIEE EVEACKTHFQ QLMESMENED KEETLAKVYI
1060 1070 1080 1090 1100
SELKNIRLRL EECEQRLLKQ IQSSASSKTD RDARQDVALR IAEQEHVQED
1110 1120 1130 1140 1150
LKHLRSDLDA VSVKCTTFLQ QSPSGSSATT LRSELNLMVE KMDHVYGLSI
1160 1170 1180 1190 1200
VCLNKLKTID VIVRSIQDAE LLVKGYEIKL SQEEAVPADL SALESHRTTL
1210 1220 1230 1240 1250
QHWLSDVKDK NSVFSVLDEE ISKAKAVAEQ LHHRAAEPNL DLERYQEKGS
1260 1270 1280 1290 1300
QLQERWHRVI AQLETRQSEV ESIQEVLRDY RACHGTLIKW IEETTAQQEM
1310 1320 1330 1340 1350
MKPGQAEDSR VLSEQLSQQT ELFAEIERNQ TKLDQCQKLS QQYSTTVKDY
1360 1370 1380 1390 1400
ELQLMTYKAF VESQQKSPGK RRRMISSSDA ITQEFMDLRT RYTALVTLTT
1410 1420 1430 1440 1450
QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKDLLGWVST LARNTQGTTT
1460 1470 1480 1490 1500
SSRTSASTDI EKAILEQQVL AEELTTKKEQ VSEAIKTSQI FLAKHGHKLS
1510 1520 1530 1540 1550
EREKEQISEQ LCALNKTYHD LCDGSANQLQ QLQSELAQQT EQKTLQKQQD
1560 1570 1580 1590 1600
TCHKKLEDLR SWVRQAERAL ERHRGRASQQ ELSALQQNQS DLKDLQGDIQ
1610 1620 1630 1640 1650
NHSTSFATAV KDIEGFLEEN QNKLSPQELT ALREKLYQAK EQYEGLQDRT
1660 1670 1680 1690 1700
REAQKELEEA VTSALQQETE KSKAATELAE NRRKIDALLD WVTSVGSSDR
1710 1720 1730 1740 1750
QPQTSLPGTE QFSGACLEKQ TLDATDGCVD VNQVPEKLDR QYELMKARHQ
1760 1770 1780 1790 1800
ELLSQQQNFI VATQSAQSFL DQHSHNLTPE ERQMLQEKLG ELKEQYAASL
1810 1820 1830 1840 1850
AQSEAKLRQT QTLRDELQKF LQDHREFENW LERSENELDG MHTGGSSPEA
1860 1870 1880 1890 1900
LNSLLKRQGS FSEDVISHKG DLRFVTISGQ KVLETENNFE EGQEPSPTRN
1910 1920 1930 1940 1950
LVNEKLKDAT ERYTTLHSKC TRLGSHLNML LGQYQQFQSS ADSLQAWMLT
1960 1970 1980 1990 2000
CEASVEKLLS DTVASDPGIL QQQLATTKQL QEELAEHQVP VEKLQKAAHD
2010 2020 2030 2040 2050
LMDIEGEPSL DCTPIRETTE SIFSRFQSLS CSLAERSALL QKAIAQSQSV
2060 2070 2080 2090 2100
QESMESLLQS MKEVEQNLEG EQVAALSSGL IQEALANNMK LKQDIARQKS
2110 2120 2130 2140 2150
SLEATREMVT RFMETADGNS AAVLQDRLAE LSQRFHRLQL QQQEKESGLK
2160 2170 2180 2190 2200
KLLPQAETFE QLSSKLQQFV EHKNRLLASG NQPDQDIAHF SQHIQELTLE
2210 2220 2230 2240 2250
MEDQKENLGT LEHLVTALGS CGFALDLSQH QEKIQNLKKD FTELQKTVQE
2260 2270 2280 2290 2300
REKDASNCQE QLDEFRKLIR TFQKWLKETE GNVPPAETFV SAKELEKQIE
2310 2320 2330 2340 2350
HLKGLLDDWA GKGVLVEEIN TKGTALESLI MDITAPDSQA KTGSVLPSVG
2360 2370 2380 2390 2400
SSVGSVNGYH TCKDLTEIQC DMSDVNSKYD KLGDALRERQ ESLQTVLSRM
2410 2420 2430 2440 2450
EEVQKEASSV LQWLESKEEV LKGMDASLSP TKTETVKAQA ESNKAFLAEL
2460 2470 2480 2490 2500
EQNSPKIQKV KEALAGLLEA YPNSQEAENW RKMQEDLNSR WEKATEVTVA
2510 2520 2530 2540 2550
RQKQLEESAS HLACFQAAES QLRPWLMEKE LMMGVLGPLS IDPNMLNAQK
2560 2570 2580 2590 2600
QQVQFMLKEF EARRQQHEQL TEAAQGILTG PGDVSPSASQ VHKDLQSISQ
2610 2620 2630 2640 2650
KWVELTDKLN SRSTQIDQAI VKSTQYQDLL QDLSEKVKAV GQRLSGQSAI
2660 2670 2680 2690 2700
STQPDAVKQQ LEETSEIRSD LGQLDDEMKE AQTLCQELSL LIGEQYLKDE
2710 2720 2730 2740 2750
LKKRLETVAL PLQGLEDLAA DRMNRLQAAL ASTQQFQQMF DELRTWLDEK
2760 2770 2780 2790 2800
QSQQAKNCPI SAKLERLQSQ LQENEEFQKN LNQHSGSYEV IVAEGESLLL
2810 2820 2830 2840 2850
SVPPGEEKKT LQNQLVELKS HWEDLNKKTV DRQSRLKDCM QKAQKYQWHV
2860 2870 2880 2890 2900
EDLVPWIKDC KSKMSELQVT LDPVQLESSL LRSKAMLNEA EKRRSLLEIL
2910 2920 2930 2940 2950
NSAADILINS SEIDEDEIRD EKAGLNQNMD AITEELQAKT GSLEEMTQRL
2960 2970 2980 2990 3000
KEFQESFKNI EKKVEGAKHQ LEIFDALGSQ ACSNKNLEKL KAQREVLQAL
3010 3020 3030 3040 3050
DPQVDYLRDF TRGLVEDAPD GSDASPLVHQ AELAQQEFLE VKQRVNSSCL
3060 3070 3080 3090 3100
TMENKLEGIG QFHCRVREMF SQLADLDDEL DGMGAIGRDT DSLQSQIEDI
3110 3120 3130 3140 3150
RLFLNKIQAL RLDIEDSEAE CRKMLEEEGT LDLLGLKREL EALNKQCGKL
3160 3170 3180 3190 3200
TERGKARQEQ LELTLGRVED FYSKLKALND AATAAEEGEA LQWIVGTEVD
3210 3220 3230 3240 3250
VINQQLADFK MFQKEQVDPL QVKLQQVNGL GQGLIQSAGK TCDVQGLEHD
3260 3270 3280 3290 3300
MEEVNTRWNT LNKKVAQRIA QLQEALLHCG KFQDALEPLL SWLTDTEELI
3310 3320 3330 3340 3350
ANQKPPSAEY KVVKAQIQEQ KLLQRLLDDR KATVDMLQAE GGRIAQAAEL
3360 3370 3380 3390 3400
ADREKITGQL ESLECRWTEL LSKAAARQKQ LEDILVLAKQ FHETAEPISD
3410 3420 3430 3440 3450
FLSVTEKKLA NSEPVGTQTA KIHQQIIRHK ALEEEIENHA ADVQQAVKIG
3460 3470 3480 3490 3500
QSLSSLICPA EQGIMSEKLD SLQARYSEIQ DRCCRKASLL EQALFNARLF
3510 3520 3530 3540 3550
GEDEVEVLNW LAEVEDKLSA VFVKDYRQDV LQKQHADHLA LNEEIINRKK
3560 3570 3580 3590 3600
NVDQAIKNGQ ALLKQTTGEE VLLIQEKLDG IKTRYADITV TSSKALRTLE
3610 3620 3630 3640 3650
QARQLATKFH STYEELTGWL REVEEELAAS GGQSPTGEQI PQFQQRQKEL
3660 3670 3680 3690 3700
KKEVMEHRLV LDTVNEVSHA LLELVPWRAR EGLDKLVSDA NEQYKLVSDT
3710 3720 3730 3740 3750
VGQRVDEIDA AIQRSQQYEQ AADAELAWVA ETKRKLMALG PIRLEQDQTT
3760 3770 3780 3790 3800
AQLQVQKAFS IDIIRHKDSM DELFSHRGEI FSTCGEEQKA VLQEKTECLI
3810 3820 3830 3840 3850
QQYEAVSLLN SERYARLERA QVLVNQFWET YEELSPWAEE TLALIAQLPP
3860 3870 3880 3890 3900
PAVDHEQLRQ QQEEMRQLRE SIAEHKPHID KILKIGPQLK ELNPEEGKMV
3910 3920 3930 3940 3950
EEKYQKAENM YAQIKDEVRQ RALALDEAVS QSAQIAEFHD KIEPMLETLE
3960 3970 3980 3990 4000
NLSSRLRMPP LIPAEVDKIR ECISDNKSAT MELEKLQPSF EALKRRGEEL
4010 4020 4030 4040 4050
IGRSQGADKD LAAKEIQDKL DQMVFFWEDI KARSEEREIK FLDVLELAEK
4060 4070 4080 4090 4100
FWYDMAALLT TIKDTQEIVH DLESPGIDPS IIKQQVEAAE TIKEETDGLH
4110 4120 4130 4140 4150
EELEFIRILG ADLIFACGET EKPEVKKSID EMNNAWENLN RTWKERLEKL
4160 4170 4180 4190 4200
EDAMQAAVQY QDTLQAMFDW LDNTVIRLCT MPPVGTDLNT VKDQLNEMKE
4210 4220 4230 4240 4250
FKVEVYQQQI EMEKLNHQGE LMLKKATDET DRDIIREPLT ELKHLWENLG
4260 4270 4280 4290 4300
EKIAHRQHKL EGALLALGQF QHALEELMGW LTHTEELLDA QRPISGDPKV
4310 4320 4330 4340 4350
IEVELAKHHV LKNDVLAHQA TVETVNKAGN ELLESSAGDD ASSLRSRLET
4360 4370 4380 4390 4400
MNQCWESVLQ KTEEREQQLQ STLQQAQGFH SEIEEFLLEL NRMESQLSAS
4410 4420 4430 4440 4450
KPTGGLPETA REQLDAHMEL HSQLRAKEEI YNQLLDKGRL MLLSRGDSGS
4460 4470 4480 4490 4500
GSKTEQSVAL LEQKWHVVSS KVEERKSKLE EALSLATEFQ NSLQEFINWL
4510 4520 4530 4540 4550
TLAEQSLNIA SPPSLILNTV LSQIEEHKVF ANEVNAHRDQ IIELDQTGNQ
4560 4570 4580 4590 4600
LKFLSQKQDV VLIKNLLVSV QSRWEKVVQR SIERGRSLDD ARKRAKQFHE
4610 4620 4630 4640 4650
AWKKLIDWLE DAESHLDSEL EISNDPDKIK LQLSKHKEFQ KTLGGKQPVY
4660 4670 4680 4690 4700
DTTIRTGRAL KEKTLLADDA QKLDNLLGEV RDKWDTVCGK SVERQHKLEE
4710 4720 4730 4740 4750
ALLFSGQFMD ALQALVDWLY KVEPQLAEDQ PVHGDLDLVM NLMDAHKVFQ
4760 4770 4780 4790 4800
KELGKRTGTV QVLKRSGREL IESSRDDTTW VKGQLQELST RWDTVCKLSV
4810 4820 4830 4840 4850
SKQSRLEQAL KQAEEFRDTV HMLLEWLSEA EQTLRFRGAL PDDTEALQSL
4860 4870 4880 4890 4900
IDTHKEFMKK VEEKRVDVNA AVAMGEVILA VCHPDCITTI KHWITIIRAR
4910 4920 4930 4940 4950
FEEVLTWAKQ HQQRLETALS ELVANAELLE ELLAWIQWAE TTLIQRDQEP
4960 4970 4980 4990 5000
IPQNIDRVKA LITEHQSFME EMTRKQPDVD RVTKTYKRKN IEPTHAPFIE
5010 5020 5030 5040 5050
KSRSGSRKSL NQPTPPPMPI LSQSEAKNPR INQLSARWQQ VWLLALERQR
5060 5070 5080 5090 5100
KLNDALDRLE ELKEFANFDF DVWRKKYMRW MNHKKSRVMD FFRRIDKDQD
5110 5120 5130 5140 5150
GKITRQEFID GILASKFPTT KLEMTAVADI FDRDGDGYID YYEFVAALHP
5160 5170 5180 5190 5200
NKDAYRPTTD ADKIEDEVTR QVAQCKCAKR FQVEQIGENK YRFGDSQQLR
5210 5220 5230 5240 5250
LVRILRSTVM VRVGGGWMAL DEFLVKNDPC RARGRTNIEL REKFILPEGA
5260 5270 5280 5290 5300
SQGMTPFRSR GRRSKPSSRA ASPTRSSSSA SQSNHSCTSM PSSPATPASG
5310 5320 5330 5340 5350
TKVISSTGSK LKRPTPTFHS SRTSLAGDTS NSSSPASTGA KTNRADPKKS
5360 5370 5380 5390 5400
ASRPGSRAGS RAGSRASSRR GSDASDFDLL ETQSACSDTS ESSAAGGQGS
5410 5420 5430
SRRGLTKPSK IPTMSKKTTT ASPRTPCPKR
Length:5,430
Mass (Da):619,600
Last modified:April 20, 2010 - v1
Checksum:iC15B030F89CD5FBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114512 Genomic DNA. No translation available.
AC131172 Genomic DNA. No translation available.
UniGeneiRn.213155.

Genome annotation databases

UCSCiRGD:1306057. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC114512 Genomic DNA. No translation available.
AC131172 Genomic DNA. No translation available.
UniGeneiRn.213155.

3D structure databases

ProteinModelPortaliD3ZHV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000041065.

PTM databases

iPTMnetiD3ZHV2.

Proteomic databases

PaxDbiD3ZHV2.
PeptideAtlasiD3ZHV2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1306057. rat.

Organism-specific databases

RGDi1306057. Macf1.

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
COG5069. LUCA.
InParanoidiD3ZHV2.

Miscellaneous databases

PROiD3ZHV2.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 2 hits.
3.30.920.20. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR003108. GAS_dom.
IPR028408. Macf1.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PANTHERiPTHR11915:SF37. PTHR11915:SF37. 5 hits.
PfamiPF00307. CH. 2 hits.
PF13499. EF-hand_7. 1 hit.
PF02187. GAS2. 1 hit.
PF00435. Spectrin. 18 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00243. GAS2. 1 hit.
SM00150. SPEC. 34 hits.
[Graphical view]
SUPFAMiSSF143575. SSF143575. 1 hit.
SSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS51460. GAR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMACF1_RAT
AccessioniPrimary (citable) accession number: D3ZHV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.