SC31A_PONAB
ID SC31A_PONAB Reviewed; 1106 AA.
AC Q5R4F4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein transport protein Sec31A;
DE AltName: Full=SEC31-like protein 1;
DE AltName: Full=SEC31-related protein A;
GN Name=SEC31A; Synonyms=SEC31L1;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER) (By similarity). The coat has two main functions, the
CC physical deformation of the endoplasmic reticulum membrane into
CC vesicles and the selection of cargo molecules (By similarity).
CC {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. SEC13 and SEC31 make a 2:2
CC tetramer that forms the edge element of the COPII outer coat. The
CC tetramer self-assembles in multiple copies to form the complete
CC polyhedral cage. Interacts (via WD 8) with SEC13 (By similarity).
CC Interacts with PDCD6; interaction takes place in response to cytosolic
CC calcium increase and leads to bridge together the BCR(KLHL12) complex
CC and SEC31A, leading to monoubiquitination. Interacts with KLHL12 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O94979}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O94979};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:O94979}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:O94979}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Associates with membranes in a GTP-dependent manner. Localizes to
CC endoplasmic reticulum exit sites (ERES), also known as transitional
CC endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q3UPL0,
CC ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- DOMAIN: The ALG-2-binding site motif-2 (ABS-2) contains a PXPGF
CC sequence that binds hydrophobic pocket 3 of PDCD6.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- PTM: Monoubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex,
CC leading to regulate the size of COPII coats.
CC {ECO:0000250|UniProtKB:O94979}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; CR861295; CAH93362.1; -; mRNA.
DR RefSeq; NP_001126980.1; NM_001133508.1.
DR AlphaFoldDB; Q5R4F4; -.
DR SMR; Q5R4F4; -.
DR GeneID; 100173999; -.
DR KEGG; pon:100173999; -.
DR CTD; 22872; -.
DR InParanoid; Q5R4F4; -.
DR OrthoDB; 100998at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 2.
DR Pfam; PF12931; Sec16_C; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation; WD repeat.
FT CHAIN 1..1106
FT /note="Protein transport protein Sec31A"
FT /id="PRO_0000295149"
FT REPEAT 4..47
FT /note="WD 1"
FT REPEAT 68..111
FT /note="WD 2"
FT REPEAT 120..160
FT /note="WD 3"
FT REPEAT 166..206
FT /note="WD 4"
FT REPEAT 209..254
FT /note="WD 5"
FT REPEAT 258..298
FT /note="WD 6"
FT REPEAT 301..342
FT /note="WD 7"
FT REPEAT 397..430
FT /note="WD 8; interaction with SEC13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 161..471
FT /note="Interaction with SEC13"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 800..999
FT /note="Interaction with PDCD6"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT REGION 859..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 842..848
FT /note="ALG-2-binding site motif-2 (ABS-2),"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT COMPBIAS 865..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1047
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
FT CROSSLNK 1103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94979"
SQ SEQUENCE 1106 AA; 121679 MW; 5BBAF2BB1B142662 CRC64;
MKLKEVDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
ATFSSSHRYH KLIWGPYKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQNDK
HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFAS SPLRVLENHA RGILAIAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSTDG LRQKQVDKLS SSFGNLDPFG
TGQPLPPLQI PQQTAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFENV RMPSHQGAEQ
QQQQHHVFIS QVVTEKEFLS RSDQLQQAVQ SQGFISYCQK KIDASQTEFE KNVWSFLKVN
FEDDSRGKYL ELLGYRKEDL GKKIALALNK VDGANVALKD SDQVAQSDGE ESPAAEEQLL
GEHIKEEKEE SEFLPSSGGT FNISVSGDID GLITQALLTG NFESAVDLCL HDNRMADAII
LAIAGGQELL ARTQKKYFAK SQSKITRLIT AVVMKNWKEI VESCDLKNWR EALAAVLTYA
KPDEFSALCD LLGTRLENEG DSLLQTQACL CYICAGNVEK LVACWTKAQD GSHPLSLQDL
IEKVVILRKA VQLTQAMDTS TVGVLLAAKM SQYANLLAAQ GSIAAALAFL PDNTNQPNIM
QLRDRLCRAQ GEPVAGHESP KIPYEEQQLP KGRPGPVAGH HQMPRVQTQQ YYPHGENPPP
PGFIMHGNVN PNAAGQLPTS PGHMHTQVPP YPQPQRPQNG WNDPPALNRV PKKKKMPENF
MPPVPITSPI MNPLGDPQSQ MLQQQPSAPV PLSSQSSFPQ PHLPGGQHFH GIQQPLGQTG
MPPSFSKPNI EGAPGAPIGN TFQHVQSLPT KKITKKPIPD EHLILKTTFE DLIQRCLSSA
TDPQTKRKLD DASKRLEFLY DKLREQTLSP TITSGLHNIA RSIETRNYSE GLTMHTHIVS
TSNFSETSAF MPVLKVVLTQ ANKLGV
