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Database: UniProt
Entry: R0KYM2_ANAPL
LinkDB: R0KYM2_ANAPL
Original site: R0KYM2_ANAPL 
ID   R0KYM2_ANAPL            Unreviewed;      1120 AA.
AC   R0KYM2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Cytospin-A {ECO:0000256|ARBA:ARBA00015657, ECO:0000256|RuleBase:RU367063};
DE   Flags: Fragment;
GN   ORFNames=Anapl_06129 {ECO:0000313|EMBL:EOA98358.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA98358.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
CC   -!- FUNCTION: Involved in cytokinesis and spindle organization. May play a
CC       role in actin cytoskeleton organization and microtubule stabilization
CC       and hence required for proper cell adhesion and migration.
CC       {ECO:0000256|ARBA:ARBA00025131, ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC       {ECO:0000256|ARBA:ARBA00011235, ECO:0000256|RuleBase:RU367063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186, ECO:0000256|RuleBase:RU367063}.
CC       Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU367063}. Cell junction,
CC       gap junction {ECO:0000256|RuleBase:RU367063}.
CC   -!- SIMILARITY: Belongs to the cytospin-A family.
CC       {ECO:0000256|ARBA:ARBA00009452, ECO:0000256|RuleBase:RU367063}.
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DR   EMBL; KB743518; EOA98358.1; -; Genomic_DNA.
DR   RefSeq; XP_005023615.1; XM_005023558.2.
DR   AlphaFoldDB; R0KYM2; -.
DR   GeneID; 101801274; -.
DR   KEGG; apla:101801274; -.
DR   CTD; 23384; -.
DR   HOGENOM; CLU_009328_1_0_1; -.
DR   OMA; HEAATYE; -.
DR   OrthoDB; 5393863at2759; -.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   CDD; cd21199; CH_CYTS; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   PANTHER; PTHR23167:SF18; CYTOSPIN-A; 1.
DR   Pfam; PF00307; CH; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|RuleBase:RU367063};
KW   Cell division {ECO:0000256|RuleBase:RU367063};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW   ECO:0000256|RuleBase:RU367063}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367063};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU367063};
KW   Gap junction {ECO:0000256|ARBA:ARBA00022868,
KW   ECO:0000256|RuleBase:RU367063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296049}.
FT   DOMAIN          1014..1119
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          1..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          414..444
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          491..808
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1120
FT                   /evidence="ECO:0000313|EMBL:EOA98358.1"
SQ   SEQUENCE   1120 AA;  125130 MW;  44C79C29639B953B CRC64;
     MKKASRSVGS VPKVPGVNKT QTTEKNKPEN GSSLSAVTKL SKTGTSASLL KTKSNDDLLA
     GMAGGGGVTM TNGVKAKKST CVSTVSSAAG TTMNSLENKP KTVAGTSSTT KRSTSSGNKE
     SSSSRERIRD RSRLSQSKKL PLTGQGTNDT VLAKRSRSRT NPESDIRMSK SKSDNQISDK
     AALEAKVNDL LTLAKTKDVE ILHLRNELRD MRAQLGLNED QVEGDEKSEE KEAIVVHQPT
     DVESTLLQLQ EQNTAIREEL NQLKNENRML KDRLNALGFS LEQRLDNSEK LFGYQSLSPE
     ITAGNHSDGG GTLTSSVEGS APGSMEDLLS QDENTLMDNQ HSNSMDNLDS ECSEVYQPLT
     SSDDALDAPS SSESEGVPSI ERSRKGSSGN ASEVSVACLT ERIHQMEENQ HSTAEELQAT
     LQELADLQQI TQELNSENER LGEEKVILME SLCQQSDKLE HFSRQIEYFR SLLDEHHISY
     VIDEDMKSGR YMELEQRYMD LAENARFERE QLLGVQQHLS NTLKMAEQDN KEAQEMIGAL
     KERNHHMERI IESEQKSKTA IASTLEEYKA TVASDQIEMN RLKAQLEHEK QKVAELYSIH
     NSGDKSDIQD LLESVRLDKE KAETLASSLQ EELAHTRNDA NRLQDAIAKV EDEYRVFQEE
     AKKQIEDLNV TLEKLRTELD EKETERSDMK ETIFELEDEV EQHRAVKLHD NLIISDLENT
     VKKLQDQKHD MEREIKNLHR RLREESAEWR QFQADLQTAV VIANDIKSEA QEEIGDLKRR
     LHEAQEKNEK LTKELEEIKS RKQEEERGRV YNYMNAVERD LAALRQGMGL SRRSSTSSEP
     TPTVKTLIKS FDSASQVPSP AAAAIPRTPL SPSPMKTPPA AAVSPMQRHS ISGPISTSKP
     LATLTDKRPS YAEIPVQEHL LRTSSTSRPA SLPRVPAMES AKSISVSRRS SEEIKRDISA
     PDGASPASLM AMGTTSPQLS LSSSPTASVT PTTRSRIREE RKDPLSALAR EYGGSKRNAL
     LKWCQKKTEG YQNIDITNFS SSWNDGLAFC AVLHTYLPAH IPYQELNSQD KRRNFTLAFQ
     AAESVGIKST LDINEMVRTE RPDWQNVMLY VTAIYKYFET
//
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