ID A0A3Q0S6G0_AMPCI Unreviewed; 1998 AA.
AC A0A3Q0S6G0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16A {ECO:0000313|Ensembl:ENSACIP00000018392.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000018392.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000018392.1}
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}.
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 STRING; 61819.ENSACIP00000018392; -.
DR Ensembl; ENSACIT00000018886.1; ENSACIP00000018392.1; ENSACIG00000014331.1.
DR GeneTree; ENSGT00940000159324; -.
DR OMA; YKSPYDL; -.
DR Proteomes; UP000261340; 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 Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1252..1350
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1422..1656
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1853..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1998 AA; 217568 MW; 99811B8B921C70F5 CRC64;
MQPPPRTGPP GATGPPPSGP NMFRRTRPYK HAAAAAPTMP PAAQPMTDPF AFSRAPPPMA
AGGLPTVPNS NPAPMQTTPN AMYPQPGSGL PPQPQVLEGA TAAPLGVNPF NPHSTAPLGP
TGYVSSHSEQ GYFNSREQTP STSTESAPVA TTSEPSQTPL NPEFQGQSAS LLVPFHPLPP
TTSSSQWAPD HGSRPPSVQN YFQPTSDPQP QPFNIPPQTQ MYPSHSPSPH HNTPTPPTQP
VHLQNQVSLP PQNPLKPPTN QWPDPNGPQQ HNSHFPTQNY FSQSSAPPDP WFNQPPQDSG
YHQMSTGMGY PQPLPDATGS QHASSTGPGP SSVPAPVPHF QESGTLSMFF KDSDVENEET
LSGERNKAAN GIAGTFQHHS NQQTHSSHAD VSSDYQGASL HDHSQVPYMN DGSRPSQGNA
QKPGDSQFDH VENLECVPNQ EVLPSEMHSS PAATAPHSVD HFETGPNLET PDSIPRPMRS
ASVSSNYSNM SHGSGTGTRR HQGVVGTFIQ QESPRLSDDP NQPAAAGGYF EQIDTSPPGD
IGVQQSSLEQ IWPPTPSPPK PTGIFQASAN SSFEPVRSHG VGVRPAEVDR AKMVAERGTD
CTPGNMEQPP DNMENIYGPG HPLPAGAGGG VPHLTHPGVH SHSRPSSRAH GINQPCESPA
TTLWAQNDPT SLGANILLAP AAPTVLAPLR EPSADVIQPP EDGPLDLQPS QRTQPSSHQH
SENLENPPKV NEAEPNDSQG NPGYATLLVP SSLHQPVFIA PPVSNYSVIP PSTTPQAVTQ
SSLRETTPPV RSVTQGHGAS TSQPPSVTCN QNPLFSPGIL SFGASASNNG PLNLTRDSTA
AATSEITVPP HPQSVRPPLS RGQSLGGDSH SALQVNLQAS LMNDLSSNHN QPSNYELLDF
SMHQSKAQTQ ASGHPSSLHE SPQSSNGFYL QVTKDAQQGL RVEANASVQT PTLSSTAQVP
PAPSQATPNT QQPPTEPPKV VDSQAALHGQ KDAPPVTAGP YRNRADPWYG RYEGQTQGYH
DPNYQYREHQ PERPSSRASQ YSDRPSSRFV KLFSLAHKMT CAVCIVCEAK VFSYVLSLFQ
MLTSCVLLHD ALHQFVFLGG FTTICNGLHF ARRKAGYDDQ WRYYPGYDAS FDDDYRRQGD
MYGDDFDRRS VHSEQSAHSV RSSHSHHSRR SSFSSRSQQS QVYRSQPDLG LVSDSTLPVD
YSYGQYPNQT DASQNYSQYY PSEYTAESTW IAPEQPPPRP ATPEKFTIPH RCARFGPGGH
LVQVLPNLPS EGQPALVDIH NLETMLQDTP EQAELRAFPG PLVKEETHKV DVIKFSQNKA
LECSRDNNLL DRDSARLLWD FIMLLCRQNG TVVGTDIADL LLKEHRSVWL PGKSPNEANL
IDFNNEPLAR AEEEPGAGPL SLLSDTFMTV PENVGKETER FRELLLFGRK KDALEAAMKG
GLWGHALLLA SKMDNRTHAR VMTRFANSLP INDPLQTVYQ LMSGRMPASA TCCGEEKWGD
WRPHLAMVLS NLSHTLDLDT RTITTMGDTL ASKGLIDAAH FCYLMAQVGL GVFTKKSTKM
VLIGSNHSLP FFQFANNEAI QRTEAYEYAQ SLGSQPCSLP NFQVFKLIYA CRLAEAGLSA
QAFHYCEVIS KTVLIQPSYY SPVFISQIIQ MSQKLRFFDP QLKEKPEQEL FVEPEWLIRL
RQLDGQIKVR RWKTPTSILQ DGMAPPQLSP SSDVPQYYPS PDMYPGAHQQ QYPPHQVGQM
SPHMHPQIPH SPIHPPAQMP LHVPPSPGHM PPVEQPPQSP VEMPTVQSIP TSPRRTSLTP
QKDFYDQMAK MVSIWQCECL NEYLYSVFGK YLVSFHTQRG VGWLGWIIGK GKNEAHLPDD
KNKSIVWDEQ KQRWVDLNEP EEESKPPPPP PSGFPKMPQV PGPGGPAAPP SSGPPVNMFS
RKAGTKSRYV DVLNPSRAAK PGGLAPAPAD IFAPLAPMPI PANLFVPSSG VXLSRSSSMS
SLSREVSQHL NQVPVAGL
//
