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Database: UniProt
Entry: I3MMC1_ICTTR
LinkDB: I3MMC1_ICTTR
Original site: I3MMC1_ICTTR 
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
//
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