ID   C2CD5_PONAB             Reviewed;        1000 AA.
AC   Q5RDC8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=C2 domain-containing protein 5;
DE   AltName: Full=138 kDa C2 domain-containing phosphoprotein;
GN   Name=C2CD5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for insulin-stimulated glucose transport and glucose
CC       transporter SLC2A4/GLUT4 translocation from intracellular glucose
CC       storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds
CC       phospholipid membranes in a calcium-dependent manner and is necessary
CC       for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC       Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00041};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}.
CC       Cytoplasm, cell cortex {ECO:0000250}. Cell membrane {ECO:0000250}. Cell
CC       projection, ruffle {ECO:0000250}. Note=Dynamically associated with
CC       GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in
CC       response to insulin stimulation. {ECO:0000250}.
CC   -!- DOMAIN: The C2 domain binds to calcium and membrane lipids.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Ser-197 by active myristoylated kinase AKT2;
CC       insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4
CC       translocation into the plasma membrane. {ECO:0000250}.
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DR   EMBL; CR857986; CAH90229.1; -; mRNA.
DR   RefSeq; NP_001125095.1; NM_001131623.1.
DR   AlphaFoldDB; Q5RDC8; -.
DR   SMR; Q5RDC8; -.
DR   GeneID; 100171977; -.
DR   KEGG; pon:100171977; -.
DR   CTD; 9847; -.
DR   InParanoid; Q5RDC8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR   GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:UniProtKB.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
DR   CDD; cd08688; C2_KIAA0528-like; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR037785; C2_C2CD5.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR038983; C2CD5.
DR   PANTHER; PTHR37412; PTHR37412; 1.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   PROSITE; PS50004; C2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW   Lipid-binding; Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..1000
FT                   /note="C2 domain-containing protein 5"
FT                   /id="PRO_0000247452"
FT   DOMAIN          1..109
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          265..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         81
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         197
FT                   /note="Phosphoserine; by PKB/AKT2"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         304
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPS5"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPS5"
FT   MOD_RES         317
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         601
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         643
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         657
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPS5"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         661
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPS5"
FT   MOD_RES         662
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         666
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         807
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
FT   MOD_RES         817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7TPS5"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86YS7"
SQ   SEQUENCE   1000 AA;  110366 MW;  FB307C795DA63C92 CRC64;
     MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV
     DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG
     EINVVVKVDL FNDLNRFRQS SCGVKFFCTT AIPKCYRAVI IHGFVEELVV NEDPEYQWID
     RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
     TACTLDKLSS PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
     SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF FTLTAFPPGF
     LVHVGGVVSA GSVKLLDRIH NPDEPETRDA WWAEIRQEIK SLAKALGCHA VVGYSESTSI
     CEEVCILSAS GTAAVLNPRF LQDGTVEGCL EQRLEENLPT RCGFCHIPYD ELNMPFPAHL
     TYCYNCRKQK VPDVLFTTID LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF
     IEYEVHTQLM NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK
     TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ RSRLLRSQSE
     SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP PSGFYSCNTE IMPGINNWTS
     EIQMFTSVRV IRLSSLNLTN QALNKNFNDL CENLLKSLYF KLRSMIPCCL CHVNFTVSLP
     EKEINQGTST ASPKNFDKKQ ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSFPSHPF
     PPAKAVTVER ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI
     RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM ENPNKNQAQC
     LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTESEVTT