SEC31_SCHPO
ID SEC31_SCHPO Reviewed; 1224 AA.
AC O13637;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Protein transport protein sec31;
GN Name=sec31; ORFNames=SPBC8D2.20c;
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 [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).
RN [3]
RP FUNCTION.
RX PubMed=11839792; DOI=10.1242/jcs.115.2.421;
RA Matynia A., Salus S.S., Sazer S.;
RT "Three proteins required for early steps in the protein secretory pathway
RT also affect nuclear envelope structure and cell cycle progression in
RT fission yeast.";
RL J. Cell Sci. 115:421-431(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499; SER-1042 AND SER-1044,
RP AND IDENTIFICATION BY 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: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11839792}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC sec23/24 complex, the sec13/31 complex, and the protein sar1. sec13 and
CC sec31 make a 2:2 tetramer that forms the edge element of the COPII
CC outer coat. The tetramer self-assembles in multiple copies to form the
CC complete polyhedral cage. Interacts (via WD 8) with sec13 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR EMBL; AB004537; BAA21425.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17835.1; -; Genomic_DNA.
DR PIR; T40765; T40765.
DR RefSeq; NP_595582.1; NM_001021477.2.
DR AlphaFoldDB; O13637; -.
DR SMR; O13637; -.
DR BioGRID; 277787; 4.
DR IntAct; O13637; 1.
DR STRING; 4896.SPBC8D2.20c.1; -.
DR iPTMnet; O13637; -.
DR MaxQB; O13637; -.
DR PaxDb; O13637; -.
DR PRIDE; O13637; -.
DR EnsemblFungi; SPBC8D2.20c.1; SPBC8D2.20c.1:pep; SPBC8D2.20c.
DR GeneID; 2541273; -.
DR KEGG; spo:SPBC8D2.20c; -.
DR PomBase; SPBC8D2.20c; sec31.
DR VEuPathDB; FungiDB:SPBC8D2.20c; -.
DR eggNOG; KOG0307; Eukaryota.
DR HOGENOM; CLU_003033_2_0_1; -.
DR InParanoid; O13637; -.
DR OMA; NRYAPAP; -.
DR PhylomeDB; O13637; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR PRO; PR:O13637; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR009917; SRA1/Sec31.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13923; PTHR13923; 2.
DR Pfam; PF07304; SRA1; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport;
KW WD repeat.
FT CHAIN 1..1224
FT /note="Protein transport protein sec31"
FT /id="PRO_0000295446"
FT REPEAT 18..57
FT /note="WD 1"
FT REPEAT 61..104
FT /note="WD 2"
FT REPEAT 114..155
FT /note="WD 3"
FT REPEAT 160..200
FT /note="WD 4"
FT REPEAT 211..254
FT /note="WD 5"
FT REPEAT 258..300
FT /note="WD 6"
FT REPEAT 302..341
FT /note="WD 7"
FT REPEAT 388..410
FT /note="WD 8; interaction with sec13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REGION 480..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1224 AA; 132499 MW; 3BF4490E8D65BF38 CRC64;
MRLKDISKTA TLAWSPRGVN DNQALLALGG YTGTEGSKNS DTLLELWNEN PESQKPVGSI
DVKTRFYDLA WEKSLDKPMG VIAGSLEDGG IGFWDPAAIL KSDEASASIA TYKSENGSIL
GPLDFNRLQP NLLASGDNKG DVWVWDIKHP QQPFALPKQN RSSEVHVVSW NNKVSHILAS
GNATEYTTVW DVKLKRQVLN LSYLGAAGVS AATGAVNSIA WHPNNATRLA TAIDDNRNPI
ILTWDLRQPT VPQNILTGHQ KAALSLSWCP EDPTFLLSSG KDGRAMVWNV ETGESLGSFP
RSGNWYTKSS WCPSNSNRVA VASLEGKVSI FSIQSTNTDK SQEASIKGAT SIDDNEFFNN
LPSIAGSQEP SFSLPLAPKW FKVPVGARFG FPNKIVSFSP NSKEVTITSA PDEVEQDEAK
SFHSSAKFQT EKEITDFCQK GVEESASEEE AINWKLLMAV SKRASRSKFA ELLGYKTLKP
KNDEDDSKVD ESVAKDSTTP NELSKNANNE NYDDDSSFYG KLAESVQEVS IADKKDAEIV
KDSFKIFNPE DSDLEKNITE ALLTGDVLSA VKACLEEKKI SEALFLSTFG GKECRKCVRD
AFYELQEHKP SYMRLSACIA DNDLQNVVDN AEVSEWKDIF VFICTYATDD EFAPLCSTLG
QRLEDLEDEK SIRSAEFCYI ASKSLQSYAN LWLKQLATST KTSKAASAYG AYVEQLTKLM
DKVSMFRSIV VYKDDELSAT KDWKLAGLYE VYIAYAKILS ASGKFDDAMS YLNLVPTEFP
GAKEEIQRLT MLLEPHAVPP IHQIKQTGYA PVQPKTSQAS SILPTVPRTT SYTSPYATTS
SHITPADVHP LPPPSTSTTA GWNDAPMLGQ LPMRRAAPSM APVRSPFPGA SSAQPAAMSR
TSSVSTLPPP PPTASMTASA PAIASPPPPK VGETYHPPTA SGTRVPPVQQ PSHPNPYTPV
APQSPVAAAS RISSSPNMPP SNPYTPIAVA SSTVNPAHTY KPHGGSQIVP PPKQPANRVV
PLPPTASQRA SAYEPPTVSV PSPSALSPSV TPQLPPVSSR LPPVSATRPQ IPQPPPVSTA
LPSSSAVSRP PIATSAGRSS TAASTSAPLT YPAGDRSHIP GNLRPIYEML NAELQRVSQS
LPPQMSRVVH DTEKRLNMLF DRLNSNVLSK PLTDELLALA TSLNAHDYQT ASNIQTNIVT
TLGDQCEHWI VGVTRLITLS KSTT
