NSG1_HUMAN
ID NSG1_HUMAN Reviewed; 185 AA.
AC P42857; B4DXC5; Q49AQ1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Neuronal vesicle trafficking-associated protein 1 {ECO:0000305};
DE AltName: Full=Neuron-enriched endosomal protein of 21 kDa {ECO:0000303|PubMed:20878061};
DE AltName: Full=Neuron-specific protein family member 1 {ECO:0000312|HGNC:HGNC:18790};
GN Name=NSG1 {ECO:0000312|HGNC:HGNC:18790};
GN Synonyms=D4S234 {ECO:0000303|PubMed:20599942},
GN NEEP21 {ECO:0000303|PubMed:20878061};
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 [GENOMIC DNA].
RX PubMed=9013775; DOI=10.1016/s0169-328x(96)00115-5;
RA Carlock L., Vo T., Lorincz M., Walker P.D., Bessert D., Wisniewski D.,
RA Dunbar J.C.;
RT "Variable subcellular localization of a neuron-specific protein during
RT NTera 2 differentiation into post-mitotic human neurons.";
RL Brain Res. Mol. Brain Res. 42:202-212(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [5]
RP INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20599942; DOI=10.1016/j.yexcr.2010.06.025;
RA Kudoh T., Kimura J., Lu Z.G., Miki Y., Yoshida K.;
RT "D4S234E, a novel p53-responsive gene, induces apoptosis in response to DNA
RT damage.";
RL Exp. Cell Res. 316:2849-2858(2010).
RN [6]
RP INDUCTION, AND FUNCTION.
RX PubMed=20878061; DOI=10.3892/ijo_00000765;
RA Ohnishi S., Futamura M., Kamino H., Nakamura Y., Kitamura N., Miyamoto Y.,
RA Miyamoto T., Shinogi D., Goda O., Arakawa H.;
RT "Identification of NEEP21, encoding neuron-enriched endosomal protein of 21
RT kDa, as a transcriptional target of tumor suppressor p53.";
RL Int. J. Oncol. 37:1133-1141(2010).
RN [7]
RP INTERACTION WITH FAM171A1.
RX PubMed=30312582; DOI=10.1016/j.ajpath.2018.09.006;
RA Rasila T., Saavalainen O., Attalla H., Lankila P., Haglund C., Hoelttae E.,
RA Andersson L.C.;
RT "Astroprincin (FAM171A1, C10orf38): A Regulator of Human Cell Shape and
RT Invasive Growth.";
RL Am. J. Pathol. 189:177-189(2019).
CC -!- FUNCTION: Plays a role in the recycling mechanism in neurons of
CC multiple receptors, including AMPAR, APP and L1CAM and acts at the
CC level of early endosomes to promote sorting of receptors toward a
CC recycling pathway. Regulates sorting and recycling of GRIA2 through
CC interaction with GRIP1 and then contributes to the regulation of
CC synaptic transmission and plasticity by affecting the recycling and
CC targeting of AMPA receptors to the synapse (By similarity). Is required
CC for faithful sorting of L1CAM to axons by facilitating trafficking from
CC somatodendritic early endosome or the recycling endosome (By
CC similarity). In an other hand, induces apoptosis via the activation of
CC CASP3 in response to DNA damage (PubMed:20599942, PubMed:20878061).
CC {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:Q62092,
CC ECO:0000269|PubMed:20599942, ECO:0000269|PubMed:20878061}.
CC -!- SUBUNIT: Forms a complex with GRIP1, GRIA2 and STX12 through direct
CC interaction with GRIP1; controls the intracellular fate of AMPAR and
CC the endosomal sorting of the GRIA2 subunit toward recycling and
CC membrane targeting. Interacts with STX12 (By similarity). Interacts
CC with APP; could regulate APP processing (By similarity). Interacts with
CC FAM171A1 (PubMed:30312582). {ECO:0000250|UniProtKB:P02683,
CC ECO:0000250|UniProtKB:Q62092, ECO:0000269|PubMed:30312582}.
CC -!- INTERACTION:
CC P42857; O75787: ATP6AP2; NbExp=3; IntAct=EBI-6380741, EBI-2512037;
CC P42857; J3KQ12: BSCL2; NbExp=5; IntAct=EBI-6380741, EBI-11532900;
CC P42857; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-6380741, EBI-10178113;
CC P42857; Q7KYR7-4: BTN2A1; NbExp=3; IntAct=EBI-6380741, EBI-17841208;
CC P42857; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-6380741, EBI-1045797;
CC P42857; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6380741, EBI-6942903;
CC P42857; P00387: CYB5R3; NbExp=3; IntAct=EBI-6380741, EBI-1046040;
CC P42857; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-6380741, EBI-781551;
CC P42857; P34910-2: EVI2B; NbExp=3; IntAct=EBI-6380741, EBI-17640610;
CC P42857; P12318-2: FCGR2A; NbExp=3; IntAct=EBI-6380741, EBI-17187481;
CC P42857; O15552: FFAR2; NbExp=3; IntAct=EBI-6380741, EBI-2833872;
CC P42857; Q96LL3: FIMP; NbExp=3; IntAct=EBI-6380741, EBI-12887376;
CC P42857; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-6380741, EBI-12142257;
CC P42857; Q99795: GPA33; NbExp=3; IntAct=EBI-6380741, EBI-4289554;
CC P42857; O15529: GPR42; NbExp=3; IntAct=EBI-6380741, EBI-18076404;
CC P42857; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-6380741, EBI-749265;
CC P42857; P43628: KIR2DL3; NbExp=3; IntAct=EBI-6380741, EBI-8632435;
CC P42857; O14880: MGST3; NbExp=3; IntAct=EBI-6380741, EBI-724754;
CC P42857; P35372-10: OPRM1; NbExp=3; IntAct=EBI-6380741, EBI-12807478;
CC P42857; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-6380741, EBI-716063;
CC P42857; O43688: PLPP2; NbExp=3; IntAct=EBI-6380741, EBI-722017;
CC P42857; Q8NC24: RELL2; NbExp=3; IntAct=EBI-6380741, EBI-10269209;
CC P42857; O14863: SLC30A4; NbExp=3; IntAct=EBI-6380741, EBI-13918058;
CC P42857; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-6380741, EBI-5235586;
CC P42857; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-6380741, EBI-17498703;
CC P42857; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-6380741, EBI-13351685;
CC P42857; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-6380741, EBI-7238458;
CC P42857; Q6UWW9: TMEM207; NbExp=3; IntAct=EBI-6380741, EBI-13301303;
CC P42857; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-6380741, EBI-3923061;
CC P42857; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-6380741, EBI-18178701;
CC P42857; Q9Y320: TMX2; NbExp=3; IntAct=EBI-6380741, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02683}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:P02683}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P02683}.
CC Endosome membrane {ECO:0000250|UniProtKB:P02683}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:P02683}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P02683}. Late endosome membrane
CC {ECO:0000250|UniProtKB:P02683}. Lysosome lumen
CC {ECO:0000250|UniProtKB:P02683}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P02683}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P02683}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P02683}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:P02683}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20599942}. Note=Endocytosed from the cell surface,
CC thus enters into early endosomes, trafficks to late endosomes and
CC degradates in lysosomes (By similarity). Endoplasmic reticulum
CC targeting is essential for apoptosis (PubMed:20599942). Found in both
CC stationary and motile endosomes. A previous study supports a type I
CC membrane protein topology (By similarity).
CC {ECO:0000250|UniProtKB:P02683, ECO:0000250|UniProtKB:Q62092,
CC ECO:0000269|PubMed:20599942}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42857-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42857-2; Sequence=VSP_054333;
CC -!- INDUCTION: Up-regulated by TP53 after DNA damage (PubMed:20599942). Up-
CC regulated by genotoxic stress (PubMed:20878061).
CC {ECO:0000269|PubMed:20599942, ECO:0000269|PubMed:20878061}.
CC -!- SIMILARITY: Belongs to the NSG family. {ECO:0000305}.
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DR EMBL; M98529; AAA60152.1; -; Genomic_DNA.
DR EMBL; M98528; AAA60355.1; -; Genomic_DNA.
DR EMBL; AK301911; BAG63337.1; -; mRNA.
DR EMBL; AC105415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001745; AAH01745.1; -; mRNA.
DR EMBL; BC034227; AAH34227.1; -; mRNA.
DR CCDS; CCDS3376.1; -. [P42857-1]
DR RefSeq; NP_001035190.1; NM_001040101.1. [P42857-1]
DR RefSeq; NP_001274692.1; NM_001287763.1. [P42857-1]
DR RefSeq; NP_055207.1; NM_014392.4. [P42857-1]
DR RefSeq; XP_016863511.1; XM_017008022.1.
DR AlphaFoldDB; P42857; -.
DR BioGRID; 117976; 34.
DR IntAct; P42857; 33.
DR STRING; 9606.ENSP00000388823; -.
DR GlyGen; P42857; 2 sites.
DR iPTMnet; P42857; -.
DR PhosphoSitePlus; P42857; -.
DR BioMuta; NSG1; -.
DR DMDM; 1168680; -.
DR MassIVE; P42857; -.
DR PaxDb; P42857; -.
DR PeptideAtlas; P42857; -.
DR PRIDE; P42857; -.
DR ProteomicsDB; 5425; -.
DR ProteomicsDB; 55560; -. [P42857-1]
DR Antibodypedia; 22570; 229 antibodies from 30 providers.
DR DNASU; 27065; -.
DR Ensembl; ENST00000397958.5; ENSP00000381049.1; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000421177.6; ENSP00000388823.2; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000433139.6; ENSP00000408833.2; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000504171.1; ENSP00000425803.1; ENSG00000168824.15. [P42857-2]
DR Ensembl; ENST00000505246.5; ENSP00000421841.1; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000506380.5; ENSP00000425423.1; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000513555.5; ENSP00000426358.1; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000513829.5; ENSP00000425345.1; ENSG00000168824.15. [P42857-1]
DR Ensembl; ENST00000621129.5; ENSP00000480081.1; ENSG00000168824.15. [P42857-1]
DR GeneID; 27065; -.
DR KEGG; hsa:27065; -.
DR MANE-Select; ENST00000621129.5; ENSP00000480081.1; NM_014392.5; NP_055207.1.
DR UCSC; uc003ghz.4; human. [P42857-1]
DR CTD; 27065; -.
DR DisGeNET; 27065; -.
DR GeneCards; NSG1; -.
DR HGNC; HGNC:18790; NSG1.
DR HPA; ENSG00000168824; Tissue enhanced (brain, pituitary gland, skin).
DR MIM; 607645; gene.
DR neXtProt; NX_P42857; -.
DR OpenTargets; ENSG00000168824; -.
DR VEuPathDB; HostDB:ENSG00000168824; -.
DR eggNOG; ENOG502QSAI; Eukaryota.
DR GeneTree; ENSGT00390000000483; -.
DR HOGENOM; CLU_112085_1_0_1; -.
DR InParanoid; P42857; -.
DR OMA; MQGRCMP; -.
DR PhylomeDB; P42857; -.
DR PathwayCommons; P42857; -.
DR SignaLink; P42857; -.
DR BioGRID-ORCS; 27065; 14 hits in 1027 CRISPR screens.
DR ChiTaRS; NSG1; human.
DR GenomeRNAi; 27065; -.
DR Pharos; P42857; Tbio.
DR PRO; PR:P42857; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42857; protein.
DR Bgee; ENSG00000168824; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; P42857; baseline and differential.
DR Genevisible; P42857; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0098845; C:postsynaptic endosome; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0099627; P:neurotransmitter receptor cycle; ISS:UniProtKB.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0099630; P:postsynaptic neurotransmitter receptor cycle; ISS:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; ISS:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0098814; P:spontaneous synaptic transmission; ISS:UniProtKB.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl.
DR InterPro; IPR009431; NSG.
DR PANTHER; PTHR28546; PTHR28546; 1.
DR Pfam; PF06387; Calcyon; 1.
DR PIRSF; PIRSF002383; Calcyon; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Lysosome; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Neuronal vesicle trafficking-associated protein 1"
FT /id="PRO_0000164363"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT TRANSMEM 83..103
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT REGION 129..164
FT /note="Required for GRIP1 interaction"
FT /evidence="ECO:0000250|UniProtKB:P02683"
FT VAR_SEQ 43..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054333"
SQ SEQUENCE 185 AA; 20913 MW; 4B7086C18BC11605 CRC64;
MVKLGNNFAE KGTKQPLLED GFDTIPLMTP LDVNQLQFPP PDKVVVKTKT EYEPDRKKGK
ARPPQIAEFT VSITEGVTER FKVSVLVLFA LAFLTCVVFL VVYKVYKYDR ACPDGFVLKN
TQCIPEGLES YYAEQDSSAR EKFYTVINHY NLAKQSITRS VSPWMSVLSE EKLSEQETEA
AEKSA
