SC31A_CHICK
ID SC31A_CHICK Reviewed; 1227 AA.
AC Q5F3X8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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; ORFNames=RCJMB04_4i13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC 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 {ECO:0000250|UniProtKB:O94979, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2Q1}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Z2Q1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z2Q1}; Peripheral membrane protein
CC {ECO:0000250}. Note=Associates with membranes in a GTP-dependent
CC manner. Localizes to endoplasmic reticulum exit sites (ERES), also
CC known as transitional endoplasmic reticulum (tER).
CC {ECO:0000250|UniProtKB:Q3UPL0, ECO:0000250|UniProtKB:Q9Z2Q1}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; AJ851522; CAH65156.1; -; mRNA.
DR RefSeq; NP_001026312.1; NM_001031141.1.
DR AlphaFoldDB; Q5F3X8; -.
DR SMR; Q5F3X8; -.
DR STRING; 9031.ENSGALP00000041556; -.
DR PaxDb; Q5F3X8; -.
DR GeneID; 422597; -.
DR KEGG; gga:422597; -.
DR CTD; 22872; -.
DR VEuPathDB; HostDB:geneid_422597; -.
DR eggNOG; KOG0307; Eukaryota.
DR InParanoid; Q5F3X8; -.
DR OrthoDB; 100998at2759; -.
DR PhylomeDB; Q5F3X8; -.
DR PRO; PR:Q5F3X8; -.
DR Proteomes; UP000000539; 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:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
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; 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 Membrane; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1227
FT /note="Protein transport protein Sec31A"
FT /id="PRO_0000295151"
FT REPEAT 4..47
FT /note="WD 1"
FT REPEAT 64..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 804..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..958
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 133470 MW; 9CCEE7A8E5C26D57 CRC64;
MKLKEIDRTA MQAWSPAQQH PIYLATGTSA QQLDASFSTN ASLEIFELDL SDPSLDMKSC
ATFSSAHRYH KLIWGPHSMT AGERVSGVLI AGGENGNVIL YDPAKIIAGD TEVIIAQKDK
HTGPVRALDV NMFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPLED ISCIAWNRQV
QHILASASPS GRATVWDLRK NEPIIKVSDH NNRMHCSGLA WHPDVATQMV LASEDDRLPV
IQMWDLRFTS SPLRVLESHT RGILAIAWSM ADSELLLSCG KDAKILCSNP NTGEVLYELP
TNMQWCFDIQ WCPRNPAILS AASFDGRLRI YSIMGGSTDG LRQKHVDQLS SSFGNLDPFG
TGQPLPPLQL PQQTAPQSVV LPLKKPPKWI RRPVGASFSF GGKLVTFENA KPQQQPGIDQ
QPQHHYVYVS QVVTEKEFLA RSTQLQEAVQ SEGFVSYCQK KVDMAQADFE RNVWSFLKVN
FEEDSRAKYL ELLGYRKDDL KNKITSALNL NKECCADGEL GEAPTESDVP LLNKGDEGQT
AEEHFLGERA KDSKQETEDL GSERKTFNIS VSGDVDGLIT QALLTGNFES AVDLCLHDNR
MADAIILAIA GGQELLSRTQ EKYFSKIQSK ITRLITAVVT KNWKEIVLSC DLQNWREALA
AVLTYARPDE FAALCDLLGN RLESEGDSLL RTQACLCYIC AGNVEKLVAC WSKVQDGNSP
LSLQDLIEKV VILRKAVQLT QAVDPNAVGA LLAEKMSQYA NLLAAQGSIA AALTFLPANT
DQPDIVLLRD RLCRAQGELP AGQEAIKAPY ERQPMPKDRA GPVAGQVPGP QASAQQYYQQ
GDKPPPPGFI MPGAINPSAP PQQATSPSYN MYSQAGTRPA YPQTYQTTQQ YSFGTGETAL
YQPQQPVAAP ASASYPSPAS NTNPPYLPAA QPVPSPLYPG QPQPSPTSLN PASSFPPPPS
GASFQHGRPG LPATSVAYAL PTGPTGTLPA ASDLPASQRT GPQNGWNDPP ALNRAAKKKK
VPDNFMPPVP ITSPIMNPLA DPQAQMQQPP AAPVGTPSFQ PQQLSTGQQA PLGPYAPQAL
GPCVVPPTTF KPRTEGAPGA PIGNAIQALP TEKITKKPIP EEHLILKTTF EALIQRCLLS
ASDPQTKRKL DDANKRLEFL YDKLREQTLS PAIVSGLHNI VKSIETRNYV EGLNIHMHIV
STSNFSETSA FMPVLKVVLI QANKLGV
