ID   C2CD5_XENTR             Reviewed;        1014 AA.
AC   Q28BX9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=C2 domain-containing protein 5;
DE   AltName: Full=138 kDa C2 domain-containing phosphoprotein;
GN   Name=c2cd5; ORFNames=TGas115n11.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be required for insulin-stimulated glucose transport and
CC       glucose transporter SLC2A4/GLUT4 translocation from intracellular
CC       glucose storage vesicle (GSV) to the plasma membrane (PM) in
CC       adipocytes. May bind phospholipid membranes in a calcium-dependent
CC       manner (By similarity). {ECO:0000250}.
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}.
CC   -!- DOMAIN: The C2 domain binds to calcium and membrane lipids.
CC       {ECO:0000250}.
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DR   EMBL; CR942580; CAJ82501.1; -; mRNA.
DR   RefSeq; NP_001039153.1; NM_001045688.1.
DR   AlphaFoldDB; Q28BX9; -.
DR   SMR; Q28BX9; -.
DR   GeneID; 733979; -.
DR   KEGG; xtr:733979; -.
DR   CTD; 9847; -.
DR   Xenbase; XB-GENE-5915013; c2cd5.
DR   eggNOG; KOG1031; Eukaryota.
DR   InParanoid; Q28BX9; -.
DR   OrthoDB; 266134at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; 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   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
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; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..1014
FT                   /note="C2 domain-containing protein 5"
FT                   /id="PRO_0000247453"
FT   DOMAIN          1..109
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          274..328
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   REGION          801..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..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   COMPBIAS        824..838
FT                   /note="Polar 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"
SQ   SEQUENCE   1014 AA;  110879 MW;  08EB2CD05D30FDD8 CRC64;
     MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYHKSLNPQ WNSEWFKFEV
     DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYTE AATVISGWFP IYDTIHGIRG
     EISVLVKVDL FNDLNRFRQS SCGVKFFCTT SIPKSYRAVV IHGFVEELVV NEDPEYQWID
     RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
     TACTLDKLSN PAPFAPSCNS PCKEIKEAPF IEELNPNTHS SGPSTPLKNQ TYSFSPSKSF
     SRQSSSSDTD LSLTPKTGMG SGSAGRDGGA FKALLRQQTQ SALEQREFPF FTLTSFPPTF
     LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHARALGCHA VVGYSESTSI
     CEEVCILSAS GTAAVLNPKF LQEASAEGCL EQRSEETSPT PCAFCHIPYD ELNMPFPANL
     TYCCACRKQK VPDVLFTTID LPSDAPVIGK GCLIQARLCR LKKKSQAEAN ATVISSLLPF
     MEYELHTQLM NKLKLKGMNG LFGLRIQITV GESMLLGLAS ATGVYLSSLP TPGGIQIAGK
     TPSEGSYDQH ISHMQKKINE TIAKNKDLYE INPPEILEET VGSPIPEPRQ RTRLLRSQSE
     SSDEAAELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVAP PPGFYSCNTE IMPGINNWIP
     NIQMFSSVRV IRLNSTNLTN QTLNKNFNDL CENLLKSLYF KLRSMVPCCL CHVNFTVAVP
     EEESIQVAVT AVAITFDKQQ ALQVPKPRPE KPQPRGSDPE EQLQFPLELS SDSPGPSTFS
     PARDVPERGG SPAGATQRAV SLDKSSPLAE SHLRHRGGGG GAIPSVTVVK MTPLSFIPGA
     KITKFLGIIN MFFIRETTSL REEGGVSGFL HAFICEVFAM VRAHVAALGG NAVVSYIMKQ
     CVFMENANKN QAQCLINVSG DAVIFISESE VEAGPGQPTA PGPQSAGVGG DSAT