ID A0A452H3V2_9SAUR Unreviewed; 457 AA.
AC A0A452H3V2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=PAT complex subunit CCDC47 {ECO:0000256|ARBA:ARBA00034875};
DE AltName: Full=Coiled-coil domain-containing protein 47 {ECO:0000256|ARBA:ARBA00034902};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000009263.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000009263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Rough endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00034697}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00034697}.
CC -!- SIMILARITY: Belongs to the CCDC47 family.
CC {ECO:0000256|ARBA:ARBA00034746}.
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DR AlphaFoldDB; A0A452H3V2; -.
DR STRING; 38772.ENSGAGP00000009263; -.
DR Ensembl; ENSGAGT00000010632.1; ENSGAGP00000009263.1; ENSGAGG00000007317.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:InterPro.
DR InterPro; IPR012879; CCDC47.
DR PANTHER; PTHR12883; ADIPOCYTE-SPECIFIC PROTEIN 4-RELATED; 1.
DR PANTHER; PTHR12883:SF0; PAT COMPLEX SUBUNIT CCDC47; 1.
DR Pfam; PF07946; CCDC47; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..457
FT /note="PAT complex subunit CCDC47"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019392801"
FT REGION 47..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 52775 MW; D40FDBB3F53F9478 CRC64;
MRSLWIFLAV LFIQWGFSLA KFDEFEDGDD IVEYDDNDFA EFEDITEDVT TESPQRIITT
EDDEEEATVE LEGHDENQED FDDADAQEGD TESEPYDDEE FEGYEEKTDA SPSKSKDPIT
IVDVPAHLQN SWESYYMEIL MVTGLLAYIM NYIIGKNKNN RLAQAWFNTH RELLESNFAL
VGDDGTNKEA ISTGKLNQEN EHIYNLWCSG RVCCEGMLIQ LKFLKRQDLL NVLARMMRPA
CDQVQIKVTM NDEDMDTYVF AVGTRKALVR LQKEMQDLSE FCSDKPKSGA KYGLPESLAI
LSEMGEITEG MMDTKMVHFL THYADKIESV HFSDQFSGPK LMQEEGQPLK LPDTKRTLLF
TFNVPGSGNT SPKDMEALLP LMNMVIYSID KAKKFRLNRE GKQKADKNRA RVEENFLKLT
HVQRQEAAQS RREEKKRAEK ERIMNEEDPE KQRRLEV
//