ANLN_XENLA
ID ANLN_XENLA Reviewed; 1116 AA.
AC Q801E2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Anillin;
GN Name=anln;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTIN; MYH9 AND MYH10, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15496454; DOI=10.1091/mbc.e04-08-0758;
RA Straight A.F., Field C.M., Mitchison T.J.;
RT "Anillin binds nonmuscle myosin II and regulates the contractile ring.";
RL Mol. Biol. Cell 16:193-201(2005).
RN [2]
RP FUNCTION, INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=12479805; DOI=10.1016/s1534-5807(02)00366-0;
RA Kinoshita M., Field C.M., Coughlin M.L., Straight A.F., Mitchison T.J.;
RT "Self- and actin-templated assembly of mammalian septins.";
RL Dev. Cell 3:791-802(2002).
CC -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC integrity of the cleavage furrow and for completion of cleavage furrow
CC ingression (PubMed:12479805). Plays a role in bleb assembly during
CC metaphase and anaphase of mitosis. May play a significant role in
CC podocyte cell migration (By similarity). {ECO:0000250|UniProtKB:Q9NQW6,
CC ECO:0000269|PubMed:12479805}.
CC -!- SUBUNIT: Interacts with and bundles F-actin (PubMed:15496454,
CC PubMed:12479805). Interacts with the non-muscle myosin II heavy chains
CC myh9 and myh10, and these interactions may be enhanced by the
CC phosphorylation of myosin II regulatory light chain by mylk
CC (PubMed:15496454). {ECO:0000269|PubMed:12479805,
CC ECO:0000269|PubMed:15496454}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:Q9NQW6}. Cell projection, bleb
CC {ECO:0000250|UniProtKB:Q9NQW6}. Note=Mainly found in the nucleus during
CC interphase. Colocalizes with cortical F-actin upon nuclear envelope
CC breakdown in mitosis and subsequently concentrates in the area of the
CC prospective contractile ring in anaphase.
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DR EMBL; AY180201; AAO31737.1; -; mRNA.
DR AlphaFoldDB; Q801E2; -.
DR SMR; Q801E2; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0032059; C:bleb; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1904172; P:positive regulation of bleb assembly; ISS:UniProtKB.
DR CDD; cd01263; PH_anillin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR031970; Anillin_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037840; PH_Anillin.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF16018; Anillin_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell cycle; Cell division; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1116
FT /note="Anillin"
FT /id="PRO_0000227967"
FT DOMAIN 975..1099
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..254
FT /note="Interactions with myh9 and myh10"
FT REGION 205..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..418
FT /note="Interaction with F-actin"
FT REGION 304..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 416..443
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 122831 MW; F53366582B677052 CRC64;
MDPFTEKLLE RTRARRENLQ KKMADRPTAG TRTAALNKRP REPLLEANHQ PPAPAEEAKP
SSKPSPSKRR CSDNASTPDA GAENKQPKTP ELPKTELSAV ASHQQLRATN QTPQVSLLSS
DKELTASDVK DASSVKTRMQ KLADQRRYWD NNVSPSSSPP AHVPPKDIIV SPPKPQIPDV
GNDTPVGRRG RFANLAATIG SWEDDLSHPF VKPNNKQEKP GTACLSKEST TSSASASMNS
HSVKQDTTSC SQRPKDTTVN KAVCSGQLKN ILPASKPASS VASTEVSGKS KPLAIKSPAV
VTSKPNENVL PASSSLKPVS ANSSPQKTER PASRIYSYQS ASARNELNNN TPVQTQQKDK
VATSGGVGIK SFLERFGEKC QEHSPAPLNQ GHRTAVLTPN TKSIQERLLK QNDISSTASL
AQQQKKEREK ELAALRGRYD RRNVWTKQED EQQGTFPETS SNLPTSDVAS CSETKRAEAS
GITSEKSVSG HFHPNMAEQV SSPEKIPTPV QSQLPLESPR LVNEGNTGNV ACEVEMSVDG
SIEEINSSGI ITNIFSDVLE QHDEEGEEVD ECLVEQVETD TDDEEREDEE EDALNISSMS
LLAPLAETVG IESPKALLSP SNKVAAGNGE SCDRKRSGRF QKSHVLRAES NDGIGSSEEN
QNLLYSIDAY RSQRFKETDR PPIMQTIVRK EDVSSRLQDK KTASPLSVNI KQKMKTLSNE
VNLQQTVIHQ ASQALNCCID EDHGKGSETE AEAERLLIVA TEKRAALIAE LNKIKNEGPQ
SQKKNVSNES APSRGCISVS EMFLPLKADF VCNATQRMDS ANYYFFLMIR AGAENIVASP
LTSITSTMKG DALAFPTTFS LEDVSNDFEI CVEVYSLVQK KEGHAPDKKK KTMKSKAITP
KRLLTSITKS NMHTPALASP GGPNAVRTSN FVLVGSHKLT LSSIGSNKFP LDKVPFLSPL
EGHIYLKIKC HVNSSVEDKG FLTMFEDVSG FGAWHRRWCV LSGYCISYWT YPDDEKRKKP
IGRINLANCT SRKIEPANRE FCARPNTFEL ITVRPQREGD RETLVSQCRD TLCVTKNWLS
ADTKEERNLW MQKLNQFLVD LRMWQPNACY RPASKP
