NVJ2_SCHPO
ID NVJ2_SCHPO Reviewed; 779 AA.
AC O94464;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Nucleus-vacuole junction protein 2 {ECO:0000312|PomBase:SPBC23G7.06c};
GN Name=nvj2 {ECO:0000312|PomBase:SPBC23G7.06c}; ORFNames=SPBC23G7.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP IDENTIFICATION OF FRAMESHIFT, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=972 / ATCC 24843, and JY3;
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: During endoplasmic reticulum (ER) stress or when cellular
CC ceramide levels increase, induces contacts between the ER and medial-
CC Golgi complex to facilitate non-vesicular transport of ceramides from
CC the ER to the Golgi complex where they are converted to complex
CC sphingolipids, preventing toxic ceramide accumulation.
CC {ECO:0000250|UniProtKB:Q06833}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC {ECO:0000305}. Nucleus membrane {ECO:0000250|UniProtKB:Q06833}; Single-
CC pass type II membrane protein {ECO:0000305}. Note=Enriched at the
CC nucleus-vacuole junction (By similarity). During endoplasmic reticulum
CC (ER) stress, localizes to ER-Golgi contacts (By similarity).
CC {ECO:0000250|UniProtKB:Q06833}.
CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind
CC various types of glycerophospholipids in its interior and mediate their
CC transfer between two adjacent bilayers. {ECO:0000255|PROSITE-
CC ProRule:PRU01194}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA22622.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAA22622.3; ALT_FRAME; Genomic_DNA.
DR PIR; T39952; T39952.
DR RefSeq; NP_595864.3; NM_001021769.3.
DR AlphaFoldDB; O94464; -.
DR STRING; 4896.SPBC23G7.06c.1; -.
DR iPTMnet; O94464; -.
DR MaxQB; O94464; -.
DR PaxDb; O94464; -.
DR PRIDE; O94464; -.
DR GeneID; 2540553; -.
DR KEGG; spo:SPBC23G7.06c; -.
DR PomBase; SPBC23G7.06c; nvj2.
DR eggNOG; KOG2238; Eukaryota.
DR HOGENOM; CLU_382245_0_0_1; -.
DR InParanoid; O94464; -.
DR PRO; PR:O94464; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071561; C:nucleus-vacuole junction; ISO:PomBase.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1990854; P:vacuole-ER tethering; ISO:PomBase.
DR InterPro; IPR031468; SMP_LBD.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid transport; Lipid-binding;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..779
FT /note="Nucleus-vacuole junction protein 2"
FT /id="PRO_0000350757"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 24..779
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT DOMAIN 238..429
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT REGION 454..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 779 AA; 87112 MW; 22D71AC88358AE34 CRC64;
MFFAFLITYL LGGVTFLPFI LFIYLLTRPT HKSEELRIIE PNNDCLTKLD KDIRIQGWIR
VTTKFLQGKS GSVKVQEIPQ DQLPKSSSDN AVTDRKTISP SGINNQYVIR NPKDVYYATV
QAGKLHLFDP VKTSELLHVI NLHEYLVVFY PGTVTENELF SNRNAIFLKY PAVSHKKESS
TKSLLNKDLY VYGRTPSNKE DWYYALLSYS KISPAIKPLE APIDFDYASV HHNLTALSSP
DTDWLNAFIG RIFLGIHKTE GFKSLVVEKL TKKLSRIKTP GIMTDVKVID VDVGEAIPTV
NGLKFESLSN GGELIVSADI WYEGDCSFKA ETTANIKFGS HFPSKTVPLA LVIRLTHVSG
KVRLLIKPPP SNRVWYAFYE KPRLHLIVEP MVARKQLTNN YLINFITQKL VELVHETIVM
PNMNDLAFFI DNEAPIKGGL WDIELFRAPT IQKPAEKDAK AERKKSGLSS STSEESLNRH
ISKRSSNSND TAPSSHIIAD KNLEPTSNIQ LKKNPDGNLV ETSELSDSDE NSVLSNKSST
LSKKVVENTS PLKYTHSASK SFIGEVQDSL QALKTKAHKP RSIGGDSSQT TLSETTKKYG
SVAKKSFFQG VSDAKSFVKK IKSTYIDDSS SNSPSDIESN YSADDNEISK SKAQNAIDFN
VTNTHSPSRS ISSEKSYKAA ERGQQDKHND VLVDLNPNVE AEKSNPHSNS QKTSKNDMSR
NQRNKYAKEI MTGQPTLHPQ GQLPIQNVEQ RATHKPLPRP PVQVETREPV RPVPPIPKL
