ID   SEC20_HUMAN             Reviewed;         228 AA.
AC   Q12981; D3DQM3; D3DQM4; D3DQM5; D3DQM6; O75622; O75623; O75624; Q6K044;
AC   Q96FG4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 3.
DT   02-JUN-2021, entry version 170.
DE   RecName: Full=Vesicle transport protein SEC20;
DE   AltName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 1;
DE   AltName: Full=Transformation-related gene 8 protein;
DE            Short=TRG-8;
GN   Name=BNIP1; Synonyms=NIP1, SEC20L; ORFNames=TRG8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH BCL2,
RP   AND INTERACTION WITH ADENOVIRUS PROTEIN E1B 19K (MICROBIAL INFECTION).
RX   PubMed=7954800; DOI=10.1016/0092-8674(94)90202-x;
RA   Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U.,
RA   Elangovan B., D'Sa-Eipper C., Chinnadurai G.;
RT   "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of
RT   cellular proteins.";
RL   Cell 79:341-351(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE SPECIFICITY.
RX   PubMed=10217402; DOI=10.1016/s0014-5793(99)00335-x;
RA   Zhang H., Heim J., Meyhack B.;
RT   "Novel BNIP1 variants and their interaction with BCL2 family members.";
RL   FEBS Lett. 448:23-27(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of human transformation-related gene.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-14.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, INTERACTION WITH NAPA; RINT1; STX18; USE1L AND ZW10, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF LEU-114.
RX   PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA   Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA   Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT   "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT   fusion.";
RL   EMBO J. 23:3216-3226(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   FUNCTION IN AUTOPHAGY, INTERACTION WITH RNF185 AND SQSTM1, SUBCELLULAR
RP   LOCATION, AND UBIQUITINATION BY RNF185.
RX   PubMed=21931693; DOI=10.1371/journal.pone.0024367;
RA   Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J., Tang J.;
RT   "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy
RT   through interaction with BNIP1.";
RL   PLoS ONE 6:E24367-E24367(2011).
RN   [10]
RP   FUNCTION, INTERACTION WITH RNF186, SUBCELLULAR LOCATION, AND UBIQUITINATION
RP   BY RNF186.
RX   PubMed=23896122; DOI=10.1016/j.cellsig.2013.07.016;
RA   Wang P., Wu Y., Li Y., Zheng J., Tang J.;
RT   "A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis
RT   through interaction with BNip1.";
RL   Cell. Signal. 25:2320-2333(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: As part of a SNARE complex may be involved in endoplasmic
CC       reticulum membranes fusion and be required for the maintenance of
CC       endoplasmic reticulum organization (PubMed:15272311). Plays also a role
CC       in apoptosis (PubMed:7954800, PubMed:15272311, PubMed:23896122). It is
CC       for instance required for endoplasmic reticulum stress-induced
CC       apoptosis (PubMed:23896122). As a substrate of RNF185 interacting with
CC       SQSTM1, might also be involved in mitochondrial autophagy (Probable).
CC       {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:23896122,
CC       ECO:0000269|PubMed:7954800, ECO:0000305|PubMed:21931693}.
CC   -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC       BNIP1/SEC20L and SEC22B (PubMed:15272311). Interacts directly with
CC       STX18, RINT1/TIP20L and NAPA (PubMed:15272311). Interacts with ZW10
CC       through RINT1 (PubMed:15272311). Interacts with BCL2 (PubMed:7954800).
CC       Interacts with RNF186 (PubMed:23896122). Interacts with RNF185
CC       (PubMed:21931693). Interacts with SQSTM1; increased by 'Lys-63'-linked
CC       polyubiquitination of BNIP1 (PubMed:21931693).
CC       {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:21931693,
CC       ECO:0000269|PubMed:23896122, ECO:0000269|PubMed:7954800}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1B 19K
CC       protein; plays a role in the suppression of cell apoptosis by the viral
CC       protein. {ECO:0000269|PubMed:7954800}.
CC   -!- INTERACTION:
CC       Q12981; P49447: CYB561; NbExp=3; IntAct=EBI-4402847, EBI-8646596;
CC       Q12981; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-4402847, EBI-18535450;
CC       Q12981; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-4402847, EBI-18636064;
CC       Q12981; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-4402847, EBI-1052304;
CC       Q12981; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-4402847, EBI-10266796;
CC       Q12981; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-4402847, EBI-2341610;
CC       Q12981; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-4402847, EBI-10192441;
CC       Q12981; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-4402847, EBI-17247926;
CC       Q12981; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-4402847, EBI-5235586;
CC       Q12981; P27105: STOM; NbExp=3; IntAct=EBI-4402847, EBI-1211440;
CC       Q12981; Q16623: STX1A; NbExp=3; IntAct=EBI-4402847, EBI-712466;
CC       Q12981; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-4402847, EBI-6448756;
CC       Q12981; Q9Y320: TMX2; NbExp=3; IntAct=EBI-4402847, EBI-6447886;
CC       Q12981; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-4402847, EBI-1055364;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:23896122}; Single-pass
CC       type IV membrane protein {ECO:0000255}. Mitochondrion membrane
CC       {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:23896122}; Single-pass
CC       type IV membrane protein {ECO:0000255}. Note=Localization to the
CC       mitochondrion is regulated by RNF186. {ECO:0000269|PubMed:23896122}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=BNIP1, S4;
CC         IsoId=Q12981-4; Sequence=Displayed;
CC       Name=2; Synonyms=BNIP1-a, S1;
CC         IsoId=Q12981-2; Sequence=VSP_004330;
CC       Name=3; Synonyms=BNIP1-b, S2;
CC         IsoId=Q12981-1; Sequence=VSP_017901;
CC       Name=4; Synonyms=BNIP1-c, S3;
CC         IsoId=Q12981-3; Sequence=VSP_017901, VSP_004330;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in heart, brain,
CC       liver skeletal muscle and pancreas. Isoform 3 is moderately expressed
CC       in placenta, lung and kidney. Isoform 4 is highly expressed in testis
CC       and small intestine. {ECO:0000269|PubMed:10217402}.
CC   -!- PTM: Polyubiquitinated (PubMed:21931693, PubMed:23896122). 'Lys-63'-
CC       linked polyubiquitination by RNF185 increases the interaction with the
CC       autophagy receptor SQSTM1 (PubMed:21931693). Undergoes 'Lys-29'- and
CC       'Lys-63'-linked polyubiquitination by RNF186 that may regulate BNIP1
CC       localization to the mitochondrion (PubMed:23896122).
CC       {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:23896122}.
CC   -!- SIMILARITY: Belongs to the SEC20 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/bnip1/";
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DR   EMBL; U15172; AAC00020.1; -; mRNA.
DR   EMBL; AF083956; AAC33124.1; -; mRNA.
DR   EMBL; AF083957; AAC33125.1; -; mRNA.
DR   EMBL; AF083958; AAC33126.1; -; mRNA.
DR   EMBL; AY216799; AAO91805.1; -; mRNA.
DR   EMBL; AY246554; AAO61090.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61405.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61406.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61408.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61409.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61410.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61411.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61412.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61413.1; -; Genomic_DNA.
DR   EMBL; BC010959; AAH10959.1; -; mRNA.
DR   CCDS; CCDS43400.1; -. [Q12981-2]
DR   CCDS; CCDS4384.1; -. [Q12981-4]
DR   CCDS; CCDS4385.1; -. [Q12981-1]
DR   CCDS; CCDS4386.1; -. [Q12981-3]
DR   PIR; I38863; I38863.
DR   RefSeq; NP_001196.2; NM_001205.2. [Q12981-4]
DR   RefSeq; NP_053581.2; NM_013978.2. [Q12981-2]
DR   RefSeq; NP_053582.2; NM_013979.2. [Q12981-1]
DR   RefSeq; NP_053583.2; NM_013980.2. [Q12981-3]
DR   SMR; Q12981; -.
DR   BioGRID; 107130; 90.
DR   IntAct; Q12981; 41.
DR   MINT; Q12981; -.
DR   iPTMnet; Q12981; -.
DR   MetOSite; Q12981; -.
DR   PhosphoSitePlus; Q12981; -.
DR   BioMuta; BNIP1; -.
DR   DMDM; 93141310; -.
DR   EPD; Q12981; -.
DR   jPOST; Q12981; -.
DR   MassIVE; Q12981; -.
DR   PeptideAtlas; Q12981; -.
DR   PRIDE; Q12981; -.
DR   ProteomicsDB; 59075; -. [Q12981-4]
DR   ProteomicsDB; 59076; -. [Q12981-1]
DR   ProteomicsDB; 59077; -. [Q12981-2]
DR   ProteomicsDB; 59078; -. [Q12981-3]
DR   Antibodypedia; 2356; 514 antibodies.
DR   DNASU; 662; -.
DR   Ensembl; ENST00000231668; ENSP00000231668; ENSG00000113734. [Q12981-1]
DR   Ensembl; ENST00000351486; ENSP00000239215; ENSG00000113734. [Q12981-4]
DR   Ensembl; ENST00000352523; ENSP00000239214; ENSG00000113734. [Q12981-3]
DR   Ensembl; ENST00000393770; ENSP00000377365; ENSG00000113734. [Q12981-2]
DR   GeneID; 662; -.
DR   KEGG; hsa:662; -.
DR   UCSC; uc003mci.5; human. [Q12981-4]
DR   CTD; 662; -.
DR   DisGeNET; 662; -.
DR   GeneCards; BNIP1; -.
DR   HGNC; HGNC:1082; BNIP1.
DR   HPA; ENSG00000113734; Low tissue specificity.
DR   MIM; 603291; gene.
DR   neXtProt; NX_Q12981; -.
DR   OpenTargets; ENSG00000113734; -.
DR   PharmGKB; PA25392; -.
DR   VEuPathDB; HostDB:ENSG00000113734.17; -.
DR   GeneTree; ENSGT00390000014412; -.
DR   HOGENOM; CLU_105902_0_0_1; -.
DR   InParanoid; Q12981; -.
DR   OMA; CVFYIVQ; -.
DR   OrthoDB; 1328108at2759; -.
DR   PhylomeDB; Q12981; -.
DR   TreeFam; TF324339; -.
DR   PathwayCommons; Q12981; -.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 662; 391 hits in 1002 CRISPR screens.
DR   ChiTaRS; BNIP1; human.
DR   GenomeRNAi; 662; -.
DR   Pharos; Q12981; Tbio.
DR   PRO; PR:Q12981; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q12981; protein.
DR   Bgee; ENSG00000113734; Expressed in secondary oocyte and 195 other tissues.
DR   ExpressionAtlas; Q12981; baseline and differential.
DR   Genevisible; Q12981; HS.
DR   GO; GO:0030137; C:COPI-coated vesicle; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:HGNC-UCL.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0031201; C:SNARE complex; IDA:HGNC-UCL.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR   GO; GO:0006915; P:apoptotic process; IPI:MGI.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:HGNC-UCL.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:HGNC-UCL.
DR   GO; GO:0097194; P:execution phase of apoptosis; IC:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0090649; P:response to oxygen-glucose deprivation; IEA:Ensembl.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   InterPro; IPR005606; Sec20.
DR   PANTHER; PTHR12825; PTHR12825; 1.
DR   Pfam; PF03908; Sec20; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Coiled coil; Endoplasmic reticulum;
KW   ER-Golgi transport; Host-virus interaction; Membrane; Mitochondrion;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..228
FT                   /note="Vesicle transport protein SEC20"
FT                   /id="PRO_0000064960"
FT   TOPO_DOM        1..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..228
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   COILED          37..90
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         59
FT                   /note="Q -> QPVLYQRAFIWTASTFFFKLTYSLTDFSSTQHDFNSPTTPVTFS
FT                   (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10217402"
FT                   /id="VSP_017901"
FT   VAR_SEQ         90..123
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10217402"
FT                   /id="VSP_004330"
FT   VARIANT         14
FT                   /note="Q -> H (in dbSNP:rs5745100)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_019169"
FT   MUTAGEN         114
FT                   /note="L->A: Loss of proapoptotic effect. No effect on
FT                   interaction with RINT1."
FT                   /evidence="ECO:0000269|PubMed:15272311"
FT   CONFLICT        14
FT                   /note="Q -> R (in Ref. 3; AAO91805)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="K -> E (in Ref. 3; AAO91805)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="A -> R (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   228 AA;  26132 MW;  23F4C21E7327DE3D CRC64;
     MAAPQDVHVR ICNQEIVKFD LEVKALIQDI RDCSGPLSAL TELNTKVKEK FQQLRHRIQD
     LEQLAKEQDK ESEKQLLLQE VENHKKQMLS NQASWRKANL TCKIAIDNLE KAELLQGGDL
     LRQRKTTKES LAQTSSTITE SLMGISRMMA QQVQQSEEAM QSLVTSSRTI LDANEEFKSM
     SGTIQLGRKL ITKYNRRELT DKLLIFLALA LFLATVLYIV KKRLFPFL
//