ID A0A3Q3EUW0_KRYMA Unreviewed; 915 AA.
AC A0A3Q3EUW0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000005477.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000005477.1}
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}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR RefSeq; XP_017289222.1; XM_017433733.1.
DR RefSeq; XP_017289223.1; XM_017433734.1.
DR AlphaFoldDB; A0A3Q3EUW0; -.
DR STRING; 37003.ENSKMAP00000005477; -.
DR Ensembl; ENSKMAT00000005574.1; ENSKMAP00000005477.1; ENSKMAG00000004166.1.
DR GeneID; 108246270; -.
DR KEGG; kmr:108246270; -.
DR CTD; 89866; -.
DR GeneTree; ENSGT00940000160138; -.
DR OMA; YAPVPMY; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000264800; 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:UP000264800};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 243..343
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 412..652
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 166..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 102156 MW; 656318460F0ED130 CRC64;
MDQRGQHLPD SSWYSHRAND SSFAQPEWDL NYRPPNLRGR SQHWGHPDPR YLAPFTRPPV
KPEWFHYNSQ QYSYGYGWQE HQRPQSRHGS EYPPHNPWDY RDSYGYYDYF RGQQAQQGTD
GGQWNPQNPR RTTKYHERTY NQEGAGNLHT KEHRYDQIKD GSQQYFNDFE DRPSKDSEEN
FSYHSGTLES SKNSGLSSSS YELSQYMNGA DLYDSDTQPA VTSGGEHGAV HQSSAPLKYS
IPHAVVSFGP AGQLVRVTPR LSTQDNVSHL EIHSMEVILS ETQEQQEMRK FPGPLTREDL
HKVDAIEFAH QKAGACVRDA TLHEGNSAAL LWNLLLLLCR QNGQVVGSDI AELLMQYSHS
DENWGSDAPT LIDFSESPTV IAPPAKGDDL LTGDLSSFSC ESPEKALQSY TDLLLAGRKK
EALESAMTSS LWGHALFLAS KMGSRSYTTV LNRFTSQLEA SDPLQTLFQL LSGRIPAVAT
CCGNEKWGDW RPHLAVMLSN ETENTAVRQK AIITMGDSLA SRGLIYAAHV CYLTASVPFG
LFTQKAERLV LLSSSHRQSF RCFATNSAIQ CTELYEYCLT FGGKCVTVPS FQVYKFLYAC
RLLDCGLSSQ AFYYCEVLGH ALLRQREPDF VLTGEVVKLS DRLRCSEAQY SETGFSGVLQ
EPEWLKCLRA RHQRLETGSY ECTEAYKPPP LRSSRACEEV CSESELDGYS CYAQGTEPEP
FYSQASEDQE RLDDQTGVHP EEMITQNWPQ TSPPSMPATV VDTPPVPTVA ISQNFSYHST
NSVEIRSSQP HSPPSNLSSA AEEAEFSFGA EKMLEVNITQ QGQHVIPPAV EGSEGATVTP
KETKTGWFRG WFKSKPNNAQ KEKSEQEGPT QTDPPPTAGH YPPPLPAALP PGTFPSQPSA
AGINPFSRKA GQQLG
//
