ID A0A2U3VSM9_ODORO Unreviewed; 1036 AA.
AC A0A2U3VSM9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16B {ECO:0000313|RefSeq:XP_004398184.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004398184.1};
RN [1] {ECO:0000313|RefSeq:XP_004398184.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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|RuleBase:RU364101}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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 RefSeq; XP_004398184.1; XM_004398127.1.
DR AlphaFoldDB; A0A2U3VSM9; -.
DR STRING; 9708.A0A2U3VSM9; -.
DR GeneID; 101373798; -.
DR KEGG; oro:101373798; -.
DR CTD; 89866; -.
DR InParanoid; A0A2U3VSM9; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000245340; 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:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
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:SF11; PROTEIN TRANSPORT PROTEIN SEC16B; 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|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW Peroxisome biogenesis {ECO:0000256|ARBA:ARBA00022593};
KW Protein transport {ECO:0000256|RuleBase:RU364101};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 273..369
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 438..672
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..1036
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 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 114418 MW; 5D4B6BB12C6CC917 CRC64;
MEFWAPQWPP QPQGRPTAPA KDPNRGLWRD GIHQPVPHSW HNGERYHQWQ DTHGSPPSQQ
DPRTDHQQPR YVSRPGERHH QPVSGVDYYE GGYPSQLYSR PGMEDPYRSY HSSTVREEYA
YGNYYYHGYP QQLQEERVPR GESPYIWQED HRDQKYLSEQ HHDNQNSLSK SQNPYKDSAA
SNSGQEWPGD LVPERLLPGT QNNKPPLADE SNLLRQHESG LSSSAYELSQ YIGNASEMYE
PRAPAAWSPV QAEDVSAAGP KEPMKFYIPH VPVSFGPGGQ LVCVGPSFPR DGQTALVELH
SMEIILNYSE EQEELRTFSG PLIREDVHKV DIMTFCQHKA AQSLKSETER SRDSALLWQL
LVLLCRQNGS MVGSDIAELL MQDCKKLEKY KRQPPVANLI NLTDEDWPVL SSGTPNLLTG
EIPPSVETPA QIIEKFTKLL YYGRKKEALE WAMKNHLWGH ALFLSSKMDP RTYNWVMSGF
TSTLAANDPL QTLFQFMSGR IPQAATCCAD KQWGDWRPHL AVILSNQGGD PELLQRAIIT
MGDTLAGKGL VEAAHFCYLM AHVPFGHYTV KTDHLALLGS NHSQEFLKFA TTEAIQRTEI
FEYCQMLGHP KSFIPSFQVY KLLYASRLAD YGLASQALHY CEAIGTALLS QEESNHPVLL
GELIKLAERL KLSDPLVVER RRGDRDPEPA WLVPLRRRCE ELVAGDTGDL RSAHSDTSGA
RGTAESTFYH DLSGHQSDSG ALGDRSALWP ALEQTWPSQP SLQQPFPHPA GGSVGQTGVP
VPLYSVPRTG GSLAVTGTPG GGAWEETQQI YPPVGENTVS QGSFQHPDSQ NVVSQPQVPA
IPRSRNNSES STVSVKEDEE ESSDEADKKS SQSPAQKEKP GDEKENTKSS GFGWFSWFRS
KPTNNASASG EDSSDGPDSE ETSRASSLPE AGPGFTLTSL PEPQSLPGTL SGATGEGQVR
GSASCGGAAE GTGSEGLSGP EAVSSELYFN PGVLLPPTPL KGSVPLYNPS QVPQLSMVSS
LNRPNRLAQR RYPTQP
//
