ICPA_DICDI
ID ICPA_DICDI Reviewed; 1320 AA.
AC Q55GF9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Inner centromere protein A;
DE AltName: Full=DdINCENP;
GN Name=icpA; Synonyms=Incenp; ORFNames=DDB_G0267690;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP AURK.
RX PubMed=16339076; DOI=10.1091/mbc.e05-08-0704;
RA Chen Q., Li H., De Lozanne A.;
RT "Contractile ring-independent localization of DdINCENP, a protein important
RT for spindle stability and cytokinesis.";
RL Mol. Biol. Cell 17:779-788(2006).
CC -!- FUNCTION: Chromosomal passenger protein that seems to be required for
CC chromosome segregation and the onset of cytokinesis during mitosis.
CC Plays a key role in the abscission of daughter cells at the end of
CC cytokinesis and in the establishment or maintenance of a bipolar
CC spindle. {ECO:0000269|PubMed:16339076}.
CC -!- SUBUNIT: Interacts with aurK. {ECO:0000269|PubMed:16339076}.
CC -!- INTERACTION:
CC Q55GF9; Q54WX4: aurK; NbExp=4; IntAct=EBI-922339, EBI-2939723;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:16339076}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:16339076}. Nucleus {ECO:0000269|PubMed:16339076}.
CC Cleavage furrow {ECO:0000269|PubMed:16339076}. Note=During mitosis,
CC found in the spindle midzone and poles. During cytokinesis, found in
CC the cleavage furrow. During prometaphase, found concentrated adjacent
CC to the condensed chromosome. During metaphase, found concentrated in
CC the middle of the spindle surrounded by chromosomes. After the onset of
CC anaphase, moved to the spindle midzone and spindle poles where it
CC remains through late telophase. After initiation of the cleavage
CC furrow, found increasingly concentrated at the furrow area, especially
CC at the cortex area. By the abscission stage of cytokinesis, found
CC highly concentrated in the thin cytoplasmic bridge connecting the two
CC daughter cells.
CC -!- DISRUPTION PHENOTYPE: Null cells divide much more slowly than wild
CC type, have a high percentage of mutant cells, become multinucleate and
CC have very enlarged nuclei. {ECO:0000269|PubMed:16339076}.
CC -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73298.1; -; Genomic_DNA.
DR RefSeq; XP_647225.1; XM_642133.1.
DR AlphaFoldDB; Q55GF9; -.
DR SMR; Q55GF9; -.
DR IntAct; Q55GF9; 3.
DR STRING; 44689.DDB0232941; -.
DR PaxDb; Q55GF9; -.
DR PRIDE; Q55GF9; -.
DR EnsemblProtists; EAL73298; EAL73298; DDB_G0267690.
DR GeneID; 8616029; -.
DR KEGG; ddi:DDB_G0267690; -.
DR dictyBase; DDB_G0267690; icpA.
DR eggNOG; ENOG502RC5R; Eukaryota.
DR HOGENOM; CLU_259973_0_0_1; -.
DR InParanoid; Q55GF9; -.
DR OMA; NGIAKPT; -.
DR PRO; PR:Q55GF9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:dictyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007059; P:chromosome segregation; IMP:dictyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:dictyBase.
DR GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR GO; GO:1905345; P:protein localization to cleavage furrow; IMP:dictyBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IDA:dictyBase.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..1320
FT /note="Inner centromere protein A"
FT /id="PRO_0000362003"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..444
FT /evidence="ECO:0000255"
FT COILED 683..855
FT /evidence="ECO:0000255"
FT COMPBIAS 611..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 152366 MW; 465CDC0BC4101861 CRC64;
MDSIKKNTIN RINGLPINHN NLSKTSIISM DDDYNSNSSF YSTNNSILNS VTKNSNYLNN
NNNNNNNNNN NNNISISNCN NNNTNNKINE QLKTFNNIFE EKGEFLKEEI DNKFNDIISL
MNQSKNQLFL SLNDIDSLYD LSPLSTTSTI TLENNNNNNN NLIKFKLFNN DSIKKYILPV
SSKTIKFKQR QILIEQQEFN EKHNQQKHLL ELQRQQVLSD QQNQFQEQHK QQLSLKQQEL
EAIQQDTNKV KQQLIETHDK LLIEKEKQFK QDLNSLELNL QNKFTNEYQS KEQEFNKKLE
QQQQQLEKQF QQTKELLIVQ ETLTLKSKLT TEFQEQLKTH QDQINKQELL LKQQEYQLFL
KQQEISSIQK QHQDDLSSLK SKLSSDQDQI KKQLLQQESD LLKKQQELLL KQQELDIQSK
QLKEEQEKQQ QQQEKQQEKQ QQQQPVVVPV KPTTSTVVSA TTATLIKAPI VSTTTVSTAT
VSKLVTNGIA KPTPLTTMKQ TVTAVPTLMD NKTRLKKLVP TATTTTTKEE NNKEYDKMMQ
ELDTQPNNSN LKNLNEKKLE TLKQQLTFDD SVSFSNGNDE SSINLSKYLE ETNKSVENTF
DIMSNTLKRK NEPIQQPSSS SSQLSSSQQP SSSSSSSSSS IGLKKRLSDD KTTIVTSKPT
NKVQPQSLNS NINNNVVPPS PVAAIANKLK KQQELEKLKL EEEERLRKKQ EEQLAKREVE
KEQERLEKKK KNDEKRKKVE ENQQQRILEE EKKKKEAEDR ELARKHKEDS DKKKREEEED
AKKRIQERFR ETQEQERKRE EFKKQQQEQE LARIKKEKLQ QEKLQQEKEK QEKQKQQQQQ
QEEEQQKKKT VQTILPTPQT PSRSANNNYD DAANTASATK AKYALSSILS MVFGATKSPH
FKPSTSQDDQ DDDDCEDYDG TDENSENEAK GEYQDDSDQE IEEQFENDSD ESMASTESNG
DIYFNKNKNS NNSNNNNDVN QSRKDKSIVF DSDSLNRNHN DSNNSSEEEE PERDPVFLTP
LPKILSNMKN NNNNNTYSNS PVIKGLSPPS SVSDYSPSSE SNDCFSPLTP TNNNKINNNK
INNNNSNNNS FNNSNSYRGL SPAQIIESHT PKCINRSGES KTSPFLTIRN TPSPLKNSPI
KFNMSSASSL SSFDSDNDSD YNDNDIDDGE ILGNPNENFT TPLKNQENNN NNNSNNSNTQ
YPIITSPPSN EDGDENYYFE EEEIDYEYDK RVPDWAKNHN LDNSLKQQRF YDPDRIFSMI
GPVYLYEIFP KQDLGGKIKD FSKVKRNLSS DWSRDCNTEK EDISYKKNMG FTNPIIVNKK
