ID   SIF2_SCHPO              Reviewed;         382 AA.
AC   O74446; Q1MTQ4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Sad1-interacting factor 2;
DE   AltName: Full=Sporulation protein sif2;
GN   Name=sif2; ORFNames=SPCC16C4.01, SPCC5E4.09;
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   INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, 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: Required for sporulation where it is believed to have a role
CC       in meiotic nuclear division. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Note=Localized primarily along the
CC       nuclear envelope in a punctate pattern. {ECO:0000269|PubMed:14655046}.
CC   -!- SIMILARITY: Belongs to the RMD1/sif2 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA21964.3; -; Genomic_DNA.
DR   PIR; T41091; T41091.
DR   PIR; T41460; T41460.
DR   RefSeq; NP_587910.3; NM_001022901.3.
DR   AlphaFoldDB; O74446; -.
DR   SMR; O74446; -.
DR   BioGRID; 275746; 30.
DR   IntAct; O74446; 1.
DR   STRING; 4896.SPCC16C4.01.1; -.
DR   iPTMnet; O74446; -.
DR   PaxDb; O74446; -.
DR   PRIDE; O74446; -.
DR   EnsemblFungi; SPCC16C4.01.1; SPCC16C4.01.1:pep; SPCC16C4.01.
DR   GeneID; 2539175; -.
DR   KEGG; spo:SPCC16C4.01; -.
DR   PomBase; SPCC16C4.01; sif2.
DR   VEuPathDB; FungiDB:SPCC16C4.01; -.
DR   eggNOG; KOG2861; Eukaryota.
DR   HOGENOM; CLU_011220_1_1_1; -.
DR   InParanoid; O74446; -.
DR   OMA; VYSQVNR; -.
DR   PhylomeDB; O74446; -.
DR   PRO; PR:O74446; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0140053; P:mitochondrial gene expression; ISO:PomBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR003734; DUF155.
DR   Pfam; PF02582; DUF155; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
PE   1: Evidence at protein level;
KW   Meiosis; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW   Sporulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..382
FT                   /note="Sad1-interacting factor 2"
FT                   /id="PRO_0000097758"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   382 AA;  44642 MW;  52153BD60ADB4512 CRC64;
     MSNRIGPQRS TKTAAKLRLL PSTEEFDDFR RQDTGREVYS QIPQIEGSTA KRDAEHLGKR
     HREFLPRVTA YCTCDTFRVD LLFKFFQSRR SSHKTRPKQF DECIYSPYSY NNEETTDLLP
     DTLESSRGTL NRESSQESLQ SIFEESGLDR NQPLFREVFC FTYGVVVLWG YTIDEEHRFL
     RELGRFEIEK LKIEDMEVEE FNYYITTLYQ PRIFNDFIAL RDASNYMIRL SISHAIAQSV
     KISLFEELVN ETIDATKDTP QMIAETGRVN LKREEIMMAV GQLFILRINI NLQGSVLDSP
     ELMWTEPQLE PIYTAARSYL EINQRVALLN QRVEVIGDLL SMLKEQITHT HDESLEWIVV
     ILMGLLVLIA LFSIVVDWKL FQ