HECA2_BOVIN
ID HECA2_BOVIN Reviewed; 491 AA.
AC A6QQC6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=HEPACAM family member 2;
DE AltName: Full=Mitotic kinetics regulator;
DE Flags: Precursor;
GN Name=HEPACAM2; Synonyms=MIKI;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required during prometaphase for centrosome maturation.
CC Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates
CC from the Golgi apparatus to mitotic centrosomes and plays a key role in
CC the formation of robust microtubules for prompt movement of
CC chromosomes: anchors AKAP9/CG-NAP, a scaffold protein of the gamma-
CC tubulin ring complex and promotes centrosome maturation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:A8MVW5}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:A8MVW5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:A8MVW5}. Midbody
CC {ECO:0000250|UniProtKB:A8MVW5}. Note=In interphase, localizes to the
CC Golgi apparatus. Localizes to centrosomes and spindles during prophase,
CC prometaphase, and metaphase of mitosis, and to midbodies at telophase.
CC Translocation to mitotic centrosomes is the result of poly-ADP-
CC ribosylation (PARsylation). {ECO:0000250|UniProtKB:A8MVW5}.
CC -!- PTM: Poly-ADP-ribosylated (PARsylated) by tankyrase TNKS during late G2
CC and prophase, leading to translocation to mitotic centrosomes.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; BC149765; AAI49766.1; -; mRNA.
DR RefSeq; NP_001095444.1; NM_001101974.1.
DR AlphaFoldDB; A6QQC6; -.
DR STRING; 9913.ENSBTAP00000016529; -.
DR PaxDb; A6QQC6; -.
DR PRIDE; A6QQC6; -.
DR Ensembl; ENSBTAT00000016529; ENSBTAP00000016529; ENSBTAG00000012456.
DR GeneID; 513430; -.
DR KEGG; bta:513430; -.
DR CTD; 253012; -.
DR VEuPathDB; HostDB:ENSBTAG00000012456; -.
DR VGNC; VGNC:29811; HEPACAM2.
DR eggNOG; ENOG502QRJQ; Eukaryota.
DR GeneTree; ENSGT01010000222242; -.
DR HOGENOM; CLU_049122_0_0_1; -.
DR InParanoid; A6QQC6; -.
DR OrthoDB; 964418at2759; -.
DR TreeFam; TF331199; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000012456; Expressed in ascending colon and 76 other tissues.
DR ExpressionAtlas; A6QQC6; baseline.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Immunoglobulin domain;
KW Membrane; Mitosis; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..491
FT /note="HEPACAM family member 2"
FT /id="PRO_0000332219"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 137..221
FT /note="Ig-like C2-type 1"
FT DOMAIN 223..319
FT /note="Ig-like C2-type 2"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 258..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 491 AA; 54561 MW; 578B8CE534EC370C CRC64;
MWLRVFTAFL SFTAGACSGL KVAVPSHTVH GIRGQALYLP VHYGFHTPAS DIQVIWLFER
PHTMPKYLLG SVNKSVVPDL EYQHKFTMMP PNASLLINPL QFTDEGNYIV KVNIQGNGTL
SASQKIQVTV DDPVTKPVVQ IQPSSGAVEY VGNMTLTCLV EGGSRRVYQW LKNGRPVHTS
STNSFSLQNS SLHIAPVTKE DIGNYSCLVK NPVSRMESDI IMPTIYYGPY GLRVNSDRGL
KVGEVFTVDI GEAILFDCSA DSYPPNTYSW IQRTNNATYV IKHGPRLEVA SEKIAQKTTD
YMCCAYNNIT GRRDETHFTV IITSVGIEKL AQKGKSLSPL ASITGISLFL IISMCLLFLW
KKFQPYKVIK QKLEGRPETE YRKARTFSGH EDALDDFGIY EFVAFPDASG VARMPARSVP
ACDGVPGQDL HSTIYEVIHH IPAQQQDHPE SSSQDGEEDA CLDRHDEAGL QELGHCKEQD
KGKHSRAKQC I
