ID   CENPI_CHICK             Reviewed;         753 AA.
AC   Q8AYS7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Centromere protein I;
DE            Short=CENP-I;
GN   Name=CENPI;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11970896; DOI=10.1016/s1534-5807(02)00144-2;
RA   Nishihashi A., Haraguchi T., Hiraoka Y., Ikemura T., Regnier V., Dodson H.,
RA   Earnshaw W.C., Fukagawa T.;
RT   "CENP-I is essential for centromere function in vertebrate cells.";
RL   Dev. Cell 2:463-476(2002).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH
RP   CENPH; CENPK; CENPL; CENPM; CENPO AND CENPP.
RX   PubMed=16622420; DOI=10.1038/ncb1396;
RA   Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA   Desai A., Fukagawa T.;
RT   "The CENP-H-I complex is required for the efficient incorporation of newly
RT   synthesized CENP-A into centromeres.";
RL   Nat. Cell Biol. 8:446-457(2006).
CC   -!- FUNCTION: Component of the CENPA-HI complex, a centromeric complex
CC       involved in assembly of kinetochore proteins, mitotic progression and
CC       chromosome segregation. Required for the localization of CENPC but not
CC       CENPA to the centromere. It however may be involved in incorporation of
CC       newly synthesized CENPA into centromeres via its interaction with the
CC       CENPA-NAC complex. {ECO:0000269|PubMed:11970896}.
CC   -!- SUBUNIT: Component of the CENPA-HI complex, at least composed of CENPH,
CC       CENPI, CENPK, CENPL, CENPM, CENPO and CENPP.
CC       {ECO:0000269|PubMed:16622420}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11970896}.
CC       Chromosome, centromere {ECO:0000269|PubMed:11970896}. Note=Localizes
CC       exclusively in the centromeres.
CC   -!- SIMILARITY: Belongs to the CENP-I/CTF3 family. {ECO:0000305}.
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DR   EMBL; AB073426; BAC22109.1; -; mRNA.
DR   RefSeq; NP_989863.1; NM_204532.1.
DR   AlphaFoldDB; Q8AYS7; -.
DR   BioGRID; 675501; 5.
DR   IntAct; Q8AYS7; 1.
DR   STRING; 9031.ENSGALP00000008063; -.
DR   PaxDb; Q8AYS7; -.
DR   Ensembl; ENSGALT00000008077; ENSGALP00000008063; ENSGALG00000005038.
DR   Ensembl; ENSGALT00000073470; ENSGALP00000055016; ENSGALG00000005038.
DR   GeneID; 395207; -.
DR   KEGG; gga:395207; -.
DR   CTD; 2491; -.
DR   VEuPathDB; HostDB:geneid_395207; -.
DR   eggNOG; ENOG502QU9H; Eukaryota.
DR   GeneTree; ENSGT00390000013235; -.
DR   HOGENOM; CLU_022189_0_0_1; -.
DR   InParanoid; Q8AYS7; -.
DR   OMA; LMDICNC; -.
DR   OrthoDB; 278624at2759; -.
DR   PhylomeDB; Q8AYS7; -.
DR   Reactome; R-GGA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:Q8AYS7; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000005038; Expressed in spermatocyte and 8 other tissues.
DR   ExpressionAtlas; Q8AYS7; baseline and differential.
DR   GO; GO:0000776; C:kinetochore; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR   InterPro; IPR012485; CENP-I.
DR   Pfam; PF07778; CENP-I; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Nucleus; Reference proteome.
FT   CHAIN           1..753
FT                   /note="Centromere protein I"
FT                   /id="PRO_0000249481"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  86894 MW;  2DD5A09D9C48FC2D CRC64;
     MQRRQSSKHS KRPLQVHHSN QTDLSAWRKG GTVDTEKSAQ NRQSLSDQKN DNEQDSLEQA
     LSYFEKIQDR VSLKKSEVLQ KHLSTMESIA LKRGLPPEGF DVLLDVALSG KLADTVNTRL
     LKSLIPASAI PESSIVSSVS WFCVSKCSSN IQLLFLRWLI TMFDFIDHKE QVHALYGIFF
     SFLNDEKLCP YICHVLYLLT RKENVKPFRV RRLLDLQSKM GMQPHLQALL SLYKLFCPEL
     VSITLPQKMK TYFKNADGPW KAAINAVRQR NQANSTVPQP LLLGTAQPHS RKRKWNTQLI
     VPASSANAQN LVVGGKMSRA DSYSANESFP VEQLRTFPQL LQNIHRLEFP SQMGSVLTNP
     LLLHYMNCSK DESVYLRLYY WMGQTLQEEC TWCVVDNNQY EEEFRGFLET VYKAECFLQE
     GFPSCEEFLY RSLPLWDGVS CRSQILQLVS WIPLSTFSEM KSQLCDPLAQ LFFTSSLYFK
     CSVLESLKEL LQNWLNWHVV QLDSESDSQF SSLNTTLSGL VNGVAELINF VGRISTAALH
     LEKSHTFLLY FILDFYETVC DIYLKYKLPL LIMPPAGVFY PALLSMDSVN LNQLCYIMYR
     YRTNLIAAKE NEMSKKKIQQ FKFSSQTYQE YNQYIIAMVG CLWTSSAFQK DNHPEGIRLD
     DELLKKTGVR EYKNSFNIVY HPALMCYAVD FLQQAWPDDT TFNFNLIKGK KWNWYLRYLY
     GQGLEGLKLF IESSINRVSK ASQSKAEDED EKV