AIN1_SCHPO
ID AIN1_SCHPO Reviewed; 621 AA.
AC O13728;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Alpha-actinin-like protein 1;
GN Name=ain1; ORFNames=SPAC15A10.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11294907; DOI=10.1091/mbc.12.4.1061;
RA Wu J.-Q., Baehler J., Pringle J.R.;
RT "Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell
RT polarization and cytokinesis.";
RL Mol. Biol. Cell 12:1061-1077(2001).
CC -!- FUNCTION: Binds to actin and is involved in actin-ring formation and
CC organization. Plays a role in cytokinesis and is involved in septation.
CC {ECO:0000269|PubMed:11294907}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11294907}. Note=Localizes to the medial ring in an
CC F-actin-dependent manner.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB10105.1; -; Genomic_DNA.
DR PIR; T37708; T37708.
DR RefSeq; NP_594295.1; NM_001019718.2.
DR PDB; 5BVR; X-ray; 1.46 A; A=1-234.
DR PDBsum; 5BVR; -.
DR AlphaFoldDB; O13728; -.
DR SMR; O13728; -.
DR BioGRID; 279253; 17.
DR STRING; 4896.SPAC15A10.08.1; -.
DR iPTMnet; O13728; -.
DR MaxQB; O13728; -.
DR PaxDb; O13728; -.
DR PRIDE; O13728; -.
DR EnsemblFungi; SPAC15A10.08.1; SPAC15A10.08.1:pep; SPAC15A10.08.
DR GeneID; 2542805; -.
DR KEGG; spo:SPAC15A10.08; -.
DR PomBase; SPAC15A10.08; ain1.
DR VEuPathDB; FungiDB:SPAC15A10.08; -.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_005217_0_2_1; -.
DR InParanoid; O13728; -.
DR OMA; QRFENVN; -.
DR PhylomeDB; O13728; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR PRO; PR:O13728; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032432; C:actin filament bundle; IDA:PomBase.
DR GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0003786; F:actin lateral binding; EXP:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:PomBase.
DR GO; GO:0051764; P:actin crosslink formation; IDA:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:PomBase.
DR GO; GO:1903478; P:actin filament bundle convergence involved in mitotic contractile ring assembly; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
DR CDD; cd00014; CH; 2.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR SMART; SM00033; CH; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Reference proteome; Repeat.
FT CHAIN 1..621
FT /note="Alpha-actinin-like protein 1"
FT /id="PRO_0000073448"
FT DOMAIN 8..114
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 123..230
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 388..419
FT /note="EF-hand 1"
FT DOMAIN 487..549
FT /note="EF-hand 2"
FT DOMAIN 550..618
FT /note="EF-hand 3"
FT REGION 86..110
FT /note="Actin-binding"
FT HELIX 9..23
FT /evidence="ECO:0007829|PDB:5BVR"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5BVR"
FT TURN 33..39
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:5BVR"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5BVR"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5BVR"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:5BVR"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:5BVR"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:5BVR"
SQ SEQUENCE 621 AA; 72443 MW; 50D7544D17942C0C CRC64;
MQANQWQSVQ NRTFTKWFNT KLSSRDLPSV FDLRKDLSDG ILLIQLLEII GDENLGRYNR
NPRMRVHRLE NVNKALEYIK SKGMPLTNIG PADIVDGNLK LILGLIWTLI LRFTIADINE
EGLTAKEGLL LWCQRKTANY HPEVDVQDFT RSWTNGLAFC ALIHQHRPDL LDYNKLDKKN
HRANMQLAFD IAQKSIGIPR LIEVEDVCDV DRPDERSIMT YVAEYFHAFS TLDKVETAAR
RVERFTEVLM STHDMKIDYE SRMKRLLGSI ARMQEYWHTV QFENNYTDVK SHSNNFAKFK
ATEKREWVKE KIDLESLLGT IQTNLKTYQL RKYEPPAGLK IVDLERQWKD FLSEEANQSK
LINTHMREIK ESMRIAFADR ANSFSKMLST ISNEITNLQG DWRDQLDHVE FLQEHLGPLE
VELASVKVLY DNCFQAGIEE NDYTMFSYED LEHEFGITAN IIANKIKYLE NELLEREKRT
LSKQELDGIT KVFRHFEKKK SNMLNEVEFY AALASLGLVY DTEEGTALFH RAANSEEGVT
YERFTEIVME ELEDRDSARQ VLYAFCDVAD GKSYVTSDDL LRSQVRPNIV KFLECNMNKH
SEGLDYLTWI KQLLAEDKEI V
