ID A0A2K6GD83_PROCO Unreviewed; 2299 AA.
AC A0A2K6GD83;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16A {ECO:0000313|Ensembl:ENSPCOP00000024191.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000024191.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000024191.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU364101}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. {ECO:0000256|RuleBase:RU364101}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004395}. 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, ECO:0000256|RuleBase:RU364101}.
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DR Ensembl; ENSPCOT00000034871.1; ENSPCOP00000024191.1; ENSPCOG00000024264.1.
DR GeneTree; ENSGT00940000159324; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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 InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402:SF13; PROTEIN TRANSPORT PROTEIN SEC16A; 1.
DR PANTHER; PTHR13402; RGPR-RELATED; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364101};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364101};
KW Golgi apparatus {ECO:0000256|RuleBase:RU364101};
KW Membrane {ECO:0000256|RuleBase:RU364101};
KW Protein transport {ECO:0000256|RuleBase:RU364101};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1435..1532
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1605..1843
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1888..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..2095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2128..2156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2225..2299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1993..2021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2299 AA; 247438 MW; 506295082C991C36 CRC64;
MQPPPQAVPS GVAGPPPAGN PQSMFWANSP YRRRTNNNVP VAPITCPLQP VTDPFAFSRQ
ALQNTPLGSL SKSSPPILQS SAPPGFPQCP GLPVPHTDAR DSSQGPCEPL PRPLSQPRAD
ASSFSGALTP SALPRAETIR SAEVRPGSEP GVQAPPYLPH YIPGVGPDTS QGTHLHGNLP
GPDQPLSRQN PPDGVVAPAA SPFSPQPCQQ MLGQWGPVQA SPQPSGQHYS PCPEGPVQSA
APHATSVPHL PPSSSPHQGV GHEQQNQLVS LSAPLASDRR SEVAHPQSGS YSANNFDPEN
TFRQNPRVGN TWASQEFRQN PGVTKEHWPA PTLVSPVTQG GHPENHVHYA PRTGASLSLP
DTDSGALSMF FQGGETENEE NLSSEKAGSA GKSDFDGFSS SPGLGHPPPL VHMAAGGICQ
GFLKGSNIET THDMWGDTAS AGTQGASSSQ CENIENLEFV QNQEVLPSES LNLDPSSPGD
QFRYGVLPGP AVPRHNVVGH TGAPEAAMHP ARSDSVSSSY SSKSHRNLSS STRPQELVGT
FIQQEVGKPE DEVSGSFFKQ IDSSPVGGET DESTVSQNYH SSVSQPSTPS PPKPTGIFQT
SANSSFEPVK SHLVGVKPVE VDRANVVGEV RGTRARQKKR RPPDASPGNL EQPPDNMETF
FAPQVCPLPV NTTAEAGHVL PHSGAPPLDT VYPTPDRKPS GRAQGMVKCE SPATTLWAQN
ELPDFGGNVL LAPAAPALQV PAKPQPSAVV QPPEEVVSGQ QSQKPSSASP LQNRDGIGAS
ENLENPPNVG EEEALQPQAS SGHADALPSP PAESLLHLPV LMAQPDQNYN LAQPVNFFVS
LSNPNGKNQS WRDASVGDKP PVDSGVLSGD SGENIPLSGI PASSVLNLSL PSSLAHSNFP
QDSGSSEMIS NQLANLLVQP PSHPLPKNLV LESQKNHNAE NVLPEFVNSP AGSTSVMLVP
PADSTVVPNS TKANHSGNRE KTYGALDFTL NRTLENPVRM YSPSRSDGLA SQHTLGNHPG
QSGPGPCNPD RFYQQVMKDA QDQPGLGGAL QELVPPQQQN SPPQVPKATS AESSNAESLP
AQGQSQNSAQ APASLAPVDT GQQLLPQASS VSLVSIGSSQ AATQSEQQWP QPTPPHTLGP
PPQDLASYYY YRPLYDGYQS QYPSLYPPDP GAASLYYPDV YGLYEPRYRP YDSTASAYAE
NYRYPEPERP SSRASHCSDR PPPRQGYPDG YYNSKSGWSS QSDYYANYYS SQYDYGGMYR
FHYSARFKDP RTCDRRYWCD VEYDPYRKEP YAYGDRPEKC DDSWRYDPRF TGSFDDNPEP
HRDPYGEEVD RRSVHSEHSA RSLRSAHSLP SRRSSLSSHS QIYRSHNVTA GSYEAPLPPG
SFRGDYAYGT YGSNFHGAQG FPEYGYAADS GWSTVEQVPS RPTSPEKFSV PHICARFGPG
GQLIKVLPNL PSEGQPALVE IHSMETLLQH TSEQEEMRAF PGPLGKGDTH KVDVINFAQN
KATKCLQDEN LIDRESASLL WNFIVLLCRQ NGTVVGTDIA ELLLRDHRTV WLPGKSPNEA
NLIDFTNEAV EHVEEEEPGE AQLSFLTDSQ PATASTLEKE TERFRELLLY GRKKDALESA
MKNGLWGHAL LLASKMDSRT HARVMTRFAN SLPINDPLQT VYQLMSGRMP AASMGPCCGQ
AYEKWGDWRP HLAMVLSNLN NNVDVESRTM ATMGDTLASK GLLDAAHFCY LMAQVGFGVY
TKKSTKLVLI GSNHSLPFSK FATNEAIQRT EAYEYARSLG AQSSPLPDFQ VFKFIYSCRL
AEMGLATQAF HYCEVIAKSI LTRPHEYSPV LISQLIQVAS QLQLFDPQLK EKPEEESFVQ
PTWLVHLQHV EKQIKEGIVV WSQDGAFPQQ CPSTPSSEVG QSDGPGLGQQ ADLETDNLLL
VVPAPSTDHL SQGVRLLPSA PQTLSDGQLA SPARVPMFPV LPSPGPLEPG PGYGLPGSAP
ALYPGPGLPP GTPSLQESRQ LQESRSTDPG TLPQEAPVGN SLSELSEEDF GGKFANLDPS
RAARDSETPT GWDRTNLGSA QPPLSLTPAP ERKRPGQAVK KEVKEPKKSE SWFSRWLPGK
KRTEAYLPDD KNKSIVWDEK KNQWVNLNEP EEEKKAPPPP PTAFPKAVQA APTGPAGVNV
FSRRAAGTRA RYVDVLNPHG TQRSEPALPP ADFFAPLAPL PIPASFAPNP GRRSEILDRM
TASCTLSFTD AEEPQLANGA GGEGQAPAGG QASPEAPGNL PSAGGTVPFY NPAQMAQASA
TSGSSRPGRI GQRKYLALN
//