HECA2_MOUSE
ID HECA2_MOUSE Reviewed; 463 AA.
AC Q4VAH7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=HEPACAM family member 2;
DE AltName: Full=Mitotic kinetics regulator;
DE Flags: Precursor;
GN Name=Hepacam2; Synonyms=Miki;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC096374; AAH96374.1; -; mRNA.
DR CCDS; CCDS39414.1; -.
DR RefSeq; NP_849230.1; NM_178899.5.
DR AlphaFoldDB; Q4VAH7; -.
DR STRING; 10090.ENSMUSP00000058882; -.
DR GlyGen; Q4VAH7; 4 sites.
DR iPTMnet; Q4VAH7; -.
DR PhosphoSitePlus; Q4VAH7; -.
DR PaxDb; Q4VAH7; -.
DR PRIDE; Q4VAH7; -.
DR ProteomicsDB; 269782; -.
DR Antibodypedia; 2717; 146 antibodies from 22 providers.
DR DNASU; 101202; -.
DR Ensembl; ENSMUST00000049985; ENSMUSP00000058882; ENSMUSG00000044156.
DR GeneID; 101202; -.
DR KEGG; mmu:101202; -.
DR UCSC; uc009auz.1; mouse.
DR CTD; 253012; -.
DR MGI; MGI:2141520; Hepacam2.
DR VEuPathDB; HostDB:ENSMUSG00000044156; -.
DR eggNOG; ENOG502QRJQ; Eukaryota.
DR GeneTree; ENSGT01010000222242; -.
DR HOGENOM; CLU_049122_0_0_1; -.
DR InParanoid; Q4VAH7; -.
DR OMA; ITPTIYY; -.
DR OrthoDB; 964418at2759; -.
DR PhylomeDB; Q4VAH7; -.
DR TreeFam; TF331199; -.
DR BioGRID-ORCS; 101202; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hepacam2; mouse.
DR PRO; PR:Q4VAH7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q4VAH7; protein.
DR Bgee; ENSMUSG00000044156; Expressed in islet of Langerhans and 66 other tissues.
DR ExpressionAtlas; Q4VAH7; baseline and differential.
DR Genevisible; Q4VAH7; MM.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..463
FT /note="HEPACAM family member 2"
FT /id="PRO_0000332221"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 150..234
FT /note="Ig-like C2-type 1"
FT DOMAIN 236..332
FT /note="Ig-like C2-type 2"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 463 AA; 51421 MW; C55981D167BC680B CRC64;
MGQDAFMELL RSMVGLSLCK IHLLLIAGSC LGLKVTVPSY TVHGIRGQAL YLPVHYGFHT
PASDIQIIWL FERSHTMPKY LLGSVNKSVV PDLEYQHKFT MMPPNASLLI NPLQFTDEGN
YIVKVNIQGN GTLSASQKIQ VTVDDPVMKP MVQFHPASGA VEYVGNITLT CQVEGGTRLV
YQWRKSGKPI SINSSHSFSP QNNTLWIVPV TKEDIGNYTC LVSNPVSEME SDIIMPTIYY
GPYGLQVNSD KGLKVGEVFT VDLGEAVLFD CSADSYPPNT YSWIQRSDNT THVIKHGPHL
EVASEKVAQK TADYVCCAYN NITGRRDETR FTVIITSVGL EKLAQRGKSL SPLASITGIS
LFLIISMCLL FLWKKYQPYK AIRQKLEGRP ESEYRKAQTF SGHEDALSDF GIYEFVTFPD
ASGVSRMSSR SSPASDGVTG QDIHGTIYEV IQHIPEQQQE NTE
