SC16B_CHICK
ID SC16B_CHICK Reviewed; 929 AA.
AC Q6AW68;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein transport protein Sec16B;
DE AltName: Full=Regucalcin gene promoter region-related protein p117;
DE Short=RGPR-p117;
DE AltName: Full=SEC16 homolog B;
GN Name=SEC16B; Synonyms=RGPR;
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 [MRNA].
RX PubMed=15583834;
RA Sawada N., Yamaguchi M.;
RT "A novel regucalcin gene promoter region-related protein: comparison of
RT nucleotide and amino acid sequences in vertebrate species.";
RL Int. J. Mol. Med. 15:97-104(2005).
CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). Required for secretory cargo traffic from the endoplasmic
CC reticulum to the Golgi apparatus. Involved in peroxisome biogenesis.
CC Regulates the transport of peroxisomal biogenesis factors PEX3 and
CC PEX16 from the ER to peroxisomes. {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96JE7}; Peripheral membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB186361; BAD34968.1; -; mRNA.
DR RefSeq; NP_001026440.1; NM_001031269.1.
DR AlphaFoldDB; Q6AW68; -.
DR STRING; 9031.ENSGALP00000007034; -.
DR PaxDb; Q6AW68; -.
DR GeneID; 424431; -.
DR KEGG; gga:424431; -.
DR CTD; 89866; -.
DR VEuPathDB; HostDB:geneid_424431; -.
DR eggNOG; KOG1913; Eukaryota.
DR InParanoid; Q6AW68; -.
DR OrthoDB; 235062at2759; -.
DR PhylomeDB; Q6AW68; -.
DR PRO; PR:Q6AW68; -.
DR Proteomes; UP000000539; Unplaced.
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:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Peroxisome biogenesis; Protein transport; Reference proteome; Transport.
FT CHAIN 1..929
FT /note="Protein transport protein Sec16B"
FT /id="PRO_0000341978"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..669
FT /note="Central conserved domain (CCD); required for
FT localization to endoplasmic reticulum exit sites"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT REGION 675..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 102956 MW; AF6863D4E9A2FAFD CRC64;
MEPWDPPQLP PVRHSHAAGS GRAEGRHGTP PPWRPIISGP LPRPGSWDPG RDLHRPASQA
ESYESGHAFR AYSRQGYEDP HWQYPGAAYR DNHAYQSHQW QPTAWQGNRD VTQVKPHGKS
TTYRDQHYYR GYHPNLAASP LGQDRSQTYD AYKEGSRRSW AGVSNLGEAS GQPQQPSLLQ
QYRESGLSSS GYELSQYIRD GAEPNDTAFL GGWSPVQGGG PLESAVMAPH KFLQPHVPVC
LGAGGQLVLV CPHRPTEGQL PLVELHSLEV ILQGTTDQEE LQAFPGPLAR EDLHKVDVMT
FCQQKIASSC DLSTQRGRDS ALLWKLLVLL CRQNGSMVGS DVAELLMQDC RQQERYKRQE
PAVGPVSLAD EEWRQLGTLD LITGEVPPVV ETQAQIVEKF TKLLYYGRKK DALVWAMRNQ
LWGHALFLSS KMDPRTYSWV LSGFTSTLAT NDPLQTFFQL MSGRIPQAAQ SCGDAKWGDW
RPHLAVLLSN KVGDMELNHR AIVTMGDTLA GKGAVEAAHF CYLMADIPFG YFGVKADRMA
LLGSSHRQAF TQFATKEAIQ RMEIFEYCQQ LRHPTSFLLP FQVYKLLYAS RLADHGLPAQ
ALLYCEQIAT VLLQQDPTSH PVLAQQLTKL AERLKLCDPL LLLEMPEQDP VLEPQWLLQL
RTYCQHCQVQ DDLAPEVALT QPEPWDTTAT PGREMVHEQP HSDGPHDEQW HQPPVPLQGP
DPHQDVSIPP LEVAVLGVGP ISQEELCTEP SLQAVPTAGD AEEPQDAHGV QQPVLAELQE
LSTRARSASE SSTASLEEDS QTSSDSPAEE LEGTSEDKSF GFRWFGWFRS KPQKETSPKA
TTSGSPTPGL QDRRSPSPPG AVPSAQPPAS PSPYRNPVSI DMKGPWDADG HEPLPGMVPL
FNPAQVSQLA AARPTQPRLL SQRRYPNPL
