TIP20_SCHPO
ID TIP20_SCHPO Reviewed; 678 AA.
AC Q9C0W8; O13625; O13626;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein transport protein tip20;
GN Name=tip20; ORFNames=pi034, SPBC691.02c;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
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).
CC -!- FUNCTION: Required for protein transport between the Golgi and the
CC endoplasmic reticulum. May contribute to tethering of coatomer-coated
CC retrograde transport vesicles to the ER membrane through interaction
CC with and stabilization of the SNARE complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of a peripheral membrane protein complex consisting
CC of dsl1, sec39/dsl3 and tip20. Bound to a SNARE complex consisting of
CC ufe1, use1, sec20 and sec22 or ykt6 through direct interaction of tip20
CC with sec20. Interacts with dsl1, sec39/dsl3 and the cytoplasmic domain
CC of sec20 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004536; BAA21413.1; -; Genomic_DNA.
DR EMBL; AB004537; BAA21414.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC37363.1; -; Genomic_DNA.
DR RefSeq; NP_595594.1; NM_001021490.2.
DR AlphaFoldDB; Q9C0W8; -.
DR SMR; Q9C0W8; -.
DR BioGRID; 277596; 4.
DR IntAct; Q9C0W8; 1.
DR STRING; 4896.SPBC691.02c.1; -.
DR iPTMnet; Q9C0W8; -.
DR SwissPalm; Q9C0W8; -.
DR MaxQB; Q9C0W8; -.
DR PaxDb; Q9C0W8; -.
DR EnsemblFungi; SPBC691.02c.1; SPBC691.02c.1:pep; SPBC691.02c.
DR GeneID; 2541081; -.
DR KEGG; spo:SPBC691.02c; -.
DR PomBase; SPBC691.02c; -.
DR VEuPathDB; FungiDB:SPBC691.02c; -.
DR eggNOG; KOG2218; Eukaryota.
DR HOGENOM; CLU_406609_0_0_1; -.
DR InParanoid; Q9C0W8; -.
DR OMA; RMCKLYS; -.
DR PhylomeDB; Q9C0W8; -.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9C0W8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070939; C:Dsl1/NZR complex; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR007528; RINT1_Tip20.
DR PANTHER; PTHR13520; PTHR13520; 1.
DR Pfam; PF04437; RINT1_TIP1; 1.
DR PROSITE; PS51386; RINT1_TIP20; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..678
FT /note="Protein transport protein tip20"
FT /id="PRO_0000116852"
FT DOMAIN 99..678
FT /note="RINT1/TIP20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00717"
SQ SEQUENCE 678 AA; 79407 MW; EE5ACAA487F0485E CRC64;
MMSQQLIDFI DSRTRHPYKS DEVEKFQQEV NELQLPDPNS LPILSEEEKR QAREDAAFRR
SSEGLEDAWL DSAIPADPTP IFRDTVELLC VYQSFVKKSA SLDTVANFLD FSTDFSTLST
KKDETEIAPD CLHYIAELLF QKKEREVKEK WKNELTEKLK TLFNWPAINP NLKESSKFES
FFGFVRSIQS FKDSETGLPL FMQVYITPYV NQFRYHFMSQ KQTNVLSKPE WFFEFLLKVF
RSNRSFYMLM RDIKFFPGVP PFFTFINLLN NVAKEKLTHI IKYDDYLVHL VHETLQYSVR
LEQHFHYTQD PLIIFLFEQN GTYDKWLGLE TQLSLTKLED IKIASDAWEL ESDQSDDFSS
AVPTKMTVRF RDMIETTFSV LQNLPSLDYQ FNFWRSVQLK PMMQYVNWLE AFYESHESSS
SIHLPGSLQT DKSKFDIAEV ERMCKLYSNF KLLMDWLDDI EDEDVYIRIG HKMGSENYAA
FYQVKPRLST LTNGSFRMIL RAVSQTLRPL LDNYSDLDTW VIKEQLPGAA LLSTSVSAEI
VGFQSRLKEI IALLQKLLIG SSQCEAIYQI GTLVESWMIK IVMTHQFSVR GGVQFAMDAM
QIVLEFSDYP LLKFERLMST VELLSLESGE NKLIKKLIIE INQKNYDFID EFFKTKEITL
SYEDALGVLY RRVDAWKD