PO152_SCHPO
ID PO152_SCHPO Reviewed; 1250 AA.
AC O94385; Q9USB0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Nucleoporin pom152;
GN Name=pom152; ORFNames=SPBC29A10.07;
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] {ECO:0000312|EMBL:CAA22435.1}
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] {ECO:0000305, ECO:0000312|EMBL:BAA87205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 311-547, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors (By similarity). {ECO:0000250|UniProtKB:P39685}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope (By similarity).
CC {ECO:0000250|UniProtKB:P39685}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:16823372}. Nucleus membrane
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass
CC type II membrane protein. Note=Central core structure of the nuclear
CC pore complex. {ECO:0000269|PubMed:16823372}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA87205.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329671; CAA22435.1; -; Genomic_DNA.
DR EMBL; AB027901; BAA87205.1; ALT_FRAME; Genomic_DNA.
DR PIR; T40062; T40062.
DR RefSeq; NP_596052.1; NM_001021963.2.
DR AlphaFoldDB; O94385; -.
DR BioGRID; 276957; 20.
DR IntAct; O94385; 1.
DR MINT; O94385; -.
DR STRING; 4896.SPBC29A10.07.1; -.
DR MaxQB; O94385; -.
DR PaxDb; O94385; -.
DR PRIDE; O94385; -.
DR EnsemblFungi; SPBC29A10.07.1; SPBC29A10.07.1:pep; SPBC29A10.07.
DR GeneID; 2540429; -.
DR KEGG; spo:SPBC29A10.07; -.
DR PomBase; SPBC29A10.07; pom152.
DR VEuPathDB; FungiDB:SPBC29A10.07; -.
DR eggNOG; ENOG502QQ5B; Eukaryota.
DR HOGENOM; CLU_002415_0_0_1; -.
DR InParanoid; O94385; -.
DR OMA; FDVFYTF; -.
DR PhylomeDB; O94385; -.
DR PRO; PR:O94385; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR InterPro; IPR037701; Pom152.
DR PANTHER; PTHR28206; PTHR28206; 1.
PE 3: Inferred from homology;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1250
FT /note="Nucleoporin pom152"
FT /id="PRO_0000224645"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..79
FT /note="Pore side"
FT /evidence="ECO:0000255"
FT REGION 101..1250
FT /note="Cisternal side"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1250 AA; 139585 MW; E409A1F2760D5D09 CRC64;
MVTRVASSER PRPLVPESIV DAPTQRLYAI GVFVALQAYK IYDLLKLETS SISDVPKSGF
LVKWIIIDAI YLRLLPKFRI PWLSFQPAAT LLQIAIFAAI NLLLSSLSSL KWISIGSILL
PYFKKKELSI SEHKINPNNV IHNSSRILGQ YTLQVLPEGT AKINPLHENY CLNSLRKDQY
VDLAIQFNST IPKYIQYSHV DLETKEETLV EVSGRSLRKL LSSSSKNPKE PRLQTIYLKT
NKRGLYTLKH VVDKSKLDVR IFRSEAVVVS CPTATFASRQ SGGRLRERCV GDTDNAELKV
TGVAPLQVTY RNWDGKHFNT HIIDSTIPDD FHPPAVVLSS NPKDIVFYKG IDIQWARSSE
IFVPINTLLK APGQWIYAVT QVTDALGNSQ QFPSNDQFLL RFAHGYTEAD GESHSLPENV
YSVFVHQRPD IQFRGCSIES PANLFPNKET SLSLYSSFSE YNSLEVGVDR YELGLDPQNI
TVPPLSHKTY QISPRSSANI NVKKPGIYVL SSVSSQYCSG EVLEPNTCLV VTPPEAKVSV
SFEEISDQCA GSIGARADLE LEGTPPFTIA YRMTKDNEAS RIQYVTTDRT RYQLNFTPKK
AGKYRYIILG IQDANYGYRE LSGSSFYKDQ TVFPLADASF EERRNGDLST VVKTSCIGDT
MSLPVLLTGS APWTLEYEIF RNNKREESHV VESKDPRYIL EVPMLVHGSQ YTITLVSVKD
SNGCKRSLNT ADTVIKVRRQ RPTATFYSSD NTYTLKSVEG ALMKIPLRLA GEKPWYVEYS
HTSGLNKVSH HKEVLNDPNS YLTVRKSGTY TLLSVSDSSC PGTIQNVEQK YQVEWLPRPF
LSIPSLESSV KGKTRYYEQN AVCAGDSSAF EVQLSGSGPF LLKHDKILVD EKSKTYPKQK
SELSTVQNTV LVKADTAVPG VYHYEFTKLS DSLYSDSDAV TIVNNQSYQA VVLQRVNSLP
KASFMNVEKL YTFCINTDVT QSNAQLIAIQ LQGASPFSLV IGIKNELTGS VSKYTLNDIH
ESVYKFAFPQ EQLTLGKHVV RLLQVRDANG CAASITKTQP AAKVSVVEMA SLAPLGSRQY
YCVGDRLSFA LQGLPPFDVE YEFNGVTQHA TSDSHILTRL IELPGVVAMK SISDHGSHCK
SYINPPIEQI VHDIPTVRIS NGKDVIENIH EGDQAEISFH FTGTPPFSFS YARRALGKKR
PGKVLETHTV TGINEYEYKV LSSVEGVYTV LSVQDKYCRY PQDSTSSSNI