ID A0A096M5K4_POEFO Unreviewed; 919 AA.
AC A0A096M5K4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000026695.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000026695.1}
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|RuleBase:RU364101}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; AYCK01005885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01005886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096M5K4; -.
DR Ensembl; ENSPFOT00000027835.1; ENSPFOP00000026695.1; ENSPFOG00000022879.1.
DR GeneTree; ENSGT00940000160138; -.
DR OMA; YAPVPMY; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 242..341
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 410..646
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 101999 MW; 63555CDD52333265 CRC64;
MDQRGHQVSD SGRRSHRKKD KEHFSRSSQQ EWDLNYPVPD QHWGRPDAHY VSHFTSPHAR
PQLLPYNSQE YAYGYGWQEH HRPQSRHGYD YSSQHHWDYQ DGYGYYDYYR GHHAQQDGVQ
WGPQESWQTN QYPDRTHVQG HGASLNSEEH RYDQRRDISQ HYLSDYETNP SRDNEEISSY
HPGTLESSKT SGLSSSSYEL SQYMNGSDVC DSDMQPVLSS DRGFLPAARQ TSVPLKYSVP
HGVVSFGPAG QLIRVTPAPT AQEKSSPLEI HSLELILSET QEQQEMRNFP GPLTREDLHK
VDAIDFAQQK AGACMRDGQL PDRRSAALLW NLLILLCRQN GQIVGSDIAE LLMQDSHSDG
SWKPEVPTLI DFDEHPAAEA PPVGGDDLLT GGPSTAGAER PERALQSYTQ LLLAGRKKEA
LESAMSSGLW GHALFLASKM GSRSYTTVLN RFTSQLVAND PLQTLFQLLS GRIPAASACC
GNEKWGDWRP HLAVMLSNET GSGAVQQKAI LTMGDSLASR GLTHAAHVCY LTAAASFGLF
PQKAERLVLL GSSHRQPFGN FASNSAIQCT ELYEYCQTLG GKSFSIPSFQ VYKVLYASRL
LDCGLSSQAF HYCEVVGQAV LRQQEPHYVL MEELIKLSDR LRFSEGHYSE AGFTAAEQEP
EWLKHLRTRH QRLQMGIYDG TDINQAVCAN HALAYKNSQL DPESDLDDLS CHNQNPEPEF
LYFQSSEHQD SLIHGSGEET QEMMSNTDTE MQQRPHADAP SMPTIAVHAP LAPAGQNFSH
HYTDGVEVRS SLPHCPLSNV SLAADVPEAD SSSGAGMMLE VSLGHSQNQR VITGAVEEPE
GPKEVPKQST KAGWFSGWFK SKPKDVQENT EKDIPAQTDQ LPAAGHHPPP PPAALPAATF
PSSPAGINPF SKRAGLEPR
//
