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Database: UniProt
Entry: A0A2K6KWS9_RHIBE
LinkDB: A0A2K6KWS9_RHIBE
Original site: A0A2K6KWS9_RHIBE 
ID   A0A2K6KWS9_RHIBE        Unreviewed;      1061 AA.
AC   A0A2K6KWS9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=SEC16 homolog B, endoplasmic reticulum export factor {ECO:0000313|Ensembl:ENSRBIP00000015720.1};
GN   Name=SEC16B {ECO:0000313|Ensembl:ENSRBIP00000015720.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000015720.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000015720.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000015720.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the SEC16 family.
CC       {ECO:0000256|ARBA:ARBA00005927}.
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DR   RefSeq; XP_017747177.1; XM_017891688.1.
DR   AlphaFoldDB; A0A2K6KWS9; -.
DR   STRING; 61621.ENSRBIP00000015720; -.
DR   Ensembl; ENSRBIT00000039564.1; ENSRBIP00000015720.1; ENSRBIG00000031958.1.
DR   GeneID; 108541921; -.
DR   CTD; 89866; -.
DR   GeneTree; ENSGT00940000160138; -.
DR   OMA; HPRDEGH; -.
DR   OrthoDB; 1361743at2759; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum 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:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR   GO; GO:0016559; P:peroxisome fission; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:Ensembl.
DR   CDD; cd09233; ACE1-Sec16-like; 1.
DR   Gene3D; 1.25.40.1030; -; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR024880; Sec16.
DR   PANTHER; PTHR13402:SF11; PROTEIN TRANSPORT PROTEIN SEC16B; 1.
DR   PANTHER; PTHR13402; RGPR-RELATED; 1.
DR   Pfam; PF12931; Sec16_C; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Transport {ECO:0000256|ARBA:ARBA00022892}.
FT   DOMAIN          447..681
FT                   /note="Ancestral coatomer element 1 Sec16/Sec31"
FT                   /evidence="ECO:0000259|Pfam:PF12931"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  116807 MW;  B57BA3E3588B45DE CRC64;
     MELWAPQRLP QTRGKVTASS KDPDGGFWRD GHHRPVPHSR HSGERFHQWQ DNRGSPQPQQ
     EPRADHQQSH YASRPGDWHQ PLSRTDYYES GYPSQLYSRP GYENSYQGYH SPTMREEYAY
     GSYYYHGHPQ WLQEERVPRQ RSPYIWHEDY REQKYLDEHH YENQHSPFGT NSETHFQSNS
     RNPYKDSPAS NSGQEWPGEL FPGSLLAGAQ KNKPSLASES NLLQQRESGL SSSSYELSQY
     ITDAPERDDP PASAAWSPVQ AEDVSSAGPK APMKFYVPHV PVSFGPGGQL VRVGPSSPTD
     GQAALVELHS MEVILNDSEE QEEMRSFSGP LIREDIHKVD IMTFCQQKAA QSCKSETLGS
     RDSALLWQLL VLLCRQNGSM VGSDIAELLM QDCKKLEKYQ RQPPVANLIS LTDEDWPVLS
     SGTPNLLTGE IPPSVETPAQ IVEKFTRLLY YGRKKEALEW AMKNHLWGHA LFLSSKMDPR
     TYSWVMSGFT STLAVNDPLQ TLFQLMSGRI PQAATCCGEK QWGDWRPHLA VILSNQAGDP
     ELYQRAIVAM GDTLAGKGLV EAAHFCYLMA HVPFGHYTVK TDHLVLLGSS HSQEFLKFAT
     TEAIQRTEIF EYCQMLGRPK SFIPSFQVYK LLYASRLADY GLVSQALHYC EAIGAAVLNQ
     GESSHPVLLA ELIKLAEKLK LSDPLVLERR SRDRDLEPDW LVQLRRQLEQ KTAGDTGDPH
     PTRSAILGAR GTTTENTFYQ DFSGCQGYSE APGYRSALWL TLEQTCLHQP SPQQPLPLQP
     GSYPAGGGAG QTGAPMPLYS VPEIHLPGTG SSVAVTEAPG GTVWEETLQT HLGPGENTVS
     QETSQPPDGQ EVISKAKTPL AARAPSISES STNSAKEDEE ESSDEADKNS PQNTARRGKL
     RDGKEHTKSP GFGWFSWFRS KPTKNASPSG EEDSSDSPDS ERETPRASSP HQAGLGLSLT
     PSPESPPLPA LSAFSIGTGG GEGRGSTSSG GAAADAGVGG LSGPESVSFE LCSNPGVLLP
     PPALKGAVPL YNPSQVPQLP MATSLNRPNR LAQRRYPTQP C
//
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