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Database: UniProt
Entry: A0A2K5TJL5_MACFA
LinkDB: A0A2K5TJL5_MACFA
Original site: A0A2K5TJL5_MACFA 
ID   A0A2K5TJL5_MACFA        Unreviewed;      1061 AA.
AC   A0A2K5TJL5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=SEC16 homolog B, endoplasmic reticulum export factor {ECO:0000313|Ensembl:ENSMFAP00000000227.2};
GN   Name=SEC16B {ECO:0000313|Ensembl:ENSMFAP00000000227.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000000227.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000000227.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000000227.2}
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   AlphaFoldDB; A0A2K5TJL5; -.
DR   STRING; 9541.ENSMFAP00000000226; -.
DR   Ensembl; ENSMFAT00000028393.2; ENSMFAP00000000227.2; ENSMFAG00000040538.2.
DR   VEuPathDB; HostDB:ENSMFAG00000040538; -.
DR   GeneTree; ENSGT00940000160138; -.
DR   OrthoDB; 1361743at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000040538; Expressed in liver and 6 other cell types or tissues.
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:UP000233100};
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..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..1014
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..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1061 AA;  116810 MW;  94340EC8DBED68B2 CRC64;
     MELWAPQRLP QTQGKVTTPS KDPDRGFRRD GHHRPVPHSR HNGERFHQWQ DNRGSPQPQQ
     EPRTDHQQSH YASRPGDWHQ PLSRIDYYKS GYPSQLYSRP GYENSYQGYH SPTTREEYAY
     GSYYYHGHPQ WLQEERVPRQ RSPYIWHEDY REQKYLDEHH YENQHSPFGT NSETHFQSNS
     RNHYKDSPAS NSGQEWPGEL FPGSLLAGAQ KTKPSLASES NLLQQRESGL SSSSYELSQY
     ITDAPERDDP PASAAWSPVQ AEDVSSAGPK APMKFYVPHA PVSFGPGGQL VCVGPSSPTD
     GQAALVELHS MEVILNDSEE QEEMRSFSGP LIREDIHKVD IMTFCQQKAA QSCKSETLGS
     RDSALLWQLL VLLCRQNGSM VGSDIAELLM QDCKKLEKYK RQPPVANLIS LTDEDWPVLS
     SGTPNLLTGE IPPSVETPAQ IVEKFTRLLY YGRKKEALEW AMKNHLWGHA LFLSSKMDPR
     TYSWVMSGFT STLALNDPLQ TLFQLMSGRI PQAATCCGEK QWGDWRPHLA VILSNQAGDP
     ELYQRAIVAM GDTLAGKGLV EAAHFCYLMA HVPFGHYTVK TDHLVLLGSS HSQEFLKFAT
     TEAIQRTEIF EYCQMLGRPK SFIPSFQVYK LLYASRLADY GLVSQALHYC EAIGAAVLSQ
     GESSHPVLLA ELIKLAEKLK LSDPLVLERR SRDRDLEPDW LVQLRRQLEQ KIAGDTGDPH
     LTRSDISGAR GTTTENTFYQ DFSGCQGYSE APEYRSALWL MLEQTCLPQP SPQQPFPLQP
     GSYPAGGGAG QTGAPMPLYS VPEIHLPGTG SSVAVTEAPG GTVWEETLQT HLGPGENTVS
     QETSQSPDGQ EVISKPQTPL AARAPSISES STNSAKEDEE ESSDEADKNS PQNTARRGKL
     GDGKEHTKSS GFGWFSWFRS KPTKNASPSG EEDSSDSPDC ERETPRASSP HQAGLGLSLT
     PSPDSPPLPA LSAFSVGTGG GEGQGSTSSG GAAAGAGVGG LSGPESVSFE LCSNPGVLLP
     PPALKGAVPL YNPSQVPQLP MATSLNRPNR LAQRRYPTQP C
//
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