ID I3MMC1_ICTTR Unreviewed; 2343 AA.
AC I3MMC1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16A {ECO:0000313|Ensembl:ENSSTOP00000012664.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000012664.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000012664.3}
RP IDENTIFICATION.
RG Ensembl;
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}. 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 EMBL; AGTP01090719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01090720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01090721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005336988.1; XM_005336931.2.
DR STRING; 43179.ENSSTOP00000012664; -.
DR Ensembl; ENSSTOT00000014137.3; ENSSTOP00000012664.3; ENSSTOG00000014119.3.
DR GeneID; 101961940; -.
DR CTD; 9919; -.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000159324; -.
DR HOGENOM; CLU_001465_0_0_1; -.
DR InParanoid; I3MMC1; -.
DR OrthoDB; 1361743at2759; -.
DR TreeFam; TF316276; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; 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 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:UP000005215};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1476..1574
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1647..1881
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2229..2343
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 120..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2244..2258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2310..2332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2343 AA; 250883 MW; 7DAACEC9D0644872 CRC64;
MQPPPQAVPS GMAGPPPAGN PRSMFWANSP HRRPASNNIP VTPISFPLQP VTDPFAFSRQ
TLQNTPLGGS SKSDLPILHS STLPAFSQWP GLPVPHTNAG DSSQGPYEPL PGPLSQPGPE
ASLLPTTSIS SLLPGPEMNR NSEVGSTSGP EVQTLPHPPH YIPGMGPDQS QGSHLHGSGS
GPDQPLNKYT PQDGAVAPAA SPLFSQPQQM PGQGAPVWGS PQPSHQHHCP CPAGLVQSIG
PQAPSAPHFP APSNLHHGLG QESHSPLVSP PEHLAAGGGN ESVRLPSGNH SASNLHPEHA
LGQNSRSRST WASQEFRQNP AANKEHLPDP AIVNTLTQGN SPENHVHYPS AAGSSRSPPE
TGSGVLSMFF QGEETENEEN LSSEKACSSG RLGFNDFSSS PALGQPLPPA HVAGGTYQAF
PKGPNTEATQ QEGDTQSYFS HSAGIQHDKQ TSKSVASVAW GDADNAGAHD ASSSRCENVE
NLEFIQNQEV LPSEPASLDP SSPSDQFRHG PLPGPAVRQS AVGLTRGEGL NLEAPEAPLH
PTRSDSVSSS YGSQSHRSLP GSARSQEPVG TFIQQEVGKP EHETAGGFFK QIGSSPIGGE
TDETTGNQNY RSSLSQPSTP SPPKPTGIFQ TSVNSSFEPV KSHLVGVKPV EADRANVVGE
VRGSRDCQKQ HRPAAAPPDA SPGNLEQPPD NMETLFAPQA CSLPHTTTTE AGYLLPHTVG
LPLDAGRPTP EKRPSARAQG ATKCESPATT LWAQDELPDF GGNVLLAPAA PALYVPAKPQ
LLAVVQPPEE GVSMQQLRKP ASAQVLQSRV GLGASENLEN PPKVGDEETL QSQAGSGYVS
LLSSPPTESL QNQPVLIAQP DQSYNLAQPI NFSVSSLNPN EKNQSWGDAL VADKSAGSNQ
ALSGDSGEHA ALSRVPTSAV TGLSLPNSLT PSNVPHSSGS SEMVANQPAS LLVQTPPHPV
PKSMLPESQN THSSAKVLPE FVSRPTGSTI ALSVPPTHGT SVFGSDEANS SSNREETVGT
LDLTLSGASG NPVRVYSPSH PDGPASQQAI ASHPRQPGPG APNPDRFYQQ VMKDAQDQAG
IERAQPELVP PQPQASLQHV PQAAFPEPSN PESPAIQGQS KNSTHPPTSP APAETGQKVP
PRPPQSSSAS AVSTSSSQAA VRSEQPWPHP PASAFGPPPQ DLASYYYYRP LYDACPPQYP
PPYPPEAGTA SLYYQDMYGL YEPRYRPYDN SAPAYTENYR YSEPERPSSR ASHCSDRPTP
RQAYPEGYYN SKSGWSSQSD YYANYYSGQY DYGDPGRWDR YYGSRFRDPR TWDRRYWYDA
EYDPHRKESY AYGDRPEKYD DHWRYDPRFT GSFDDDTEPP RDPYGEEVDR RSVHSEHSAR
SLRSAHSLPS RRSSLSSHSH QSQIFRSHNV TTGSFEVPPP PGSFHGDYAY GTYGSNFGSA
HGFPEYSYPA DTGWPAVDQV PSRPTSPEKF SVPHICAKFG PGGQLIKVIP NLPSEGQPAL
VEIHSMETLL QHTPEQEELR SFPGPLGKDD THKVDVINFA QNKATKCLQN ENLMDKESAS
LLWNLIILLC RQNGTVVGTD IAELLLRDHR TVWLPGKSPN EANLIDFTNE AVEQVQEEES
GEAQLSFLTD SQTASTSTLE KETERFRELL LYGRKKDALE SAMKNGLWGH ALLLASKMDS
RTHARVMTRF ANSLPINDPL QTVYQLMSGR MPAASTCCGD EKWGDWRPHL AMVLSNLNNN
MDVESRTMAT MGDTLASKGL LDAAHFCYLM AQVGFGVYTK KTTKLVLIGS NHSLPFLKFA
TNEAIQRTEA YEYAQSLGAQ TSALPHFQVF KFIYSCRLAE MGLATQAFHY CEVIAKSILT
QPAAYSAVLI SQLVQMSSQL RLFDPQLREK PEEESFIEPA WLVQLQRVER QIQEGAVPWN
QDGADPQECP STPGSEVDQL DAPVQGQPSG LGADQPLLMP STEPSSQGVH LLASAPQMLP
DGQLAHSARV PMFPVSPPTG ALESGPGCGP PVSAVGFSEP SRPDPAALYT GLGLPPGVPS
LQESGSLLQE SRSLDPGMVP QDAPVGNVFP KPSEEDFGGN FADLGSSRTA QDAETPPAWD
PTSSASAQSA SSLSPASETK RPAHVARKET KEPKKSESWF SRWLPGKKRT EAYLPDDKNK
SIVWDEKKNQ WVNLNEPEEE KKAPPPPPTS LPRASHVAPP GLTGPPTASV NMFSRKAGGS
RARYVDVLNP SGASRGEPAP APADFFAPLA PLPIPSNLFT PSPDAEEPHL AEGAGRVGPG
PAGAQANLEP TTEPKAPGDH CPAGNPPSGT VPFYSPSQLA QASTSSGSSR PGRIGQRKYP
ALN
//