PAN1_SCHPO
ID PAN1_SCHPO Reviewed; 1794 AA.
AC Q10172; Q9USC5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=SPAC25G10.09c, SPAC27F1.01c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 94-281.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152; THR-706; SER-1219;
RP SER-1221; SER-1406; SER-1409; SER-1412 AND SER-1414, 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: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA94638.1; -; Genomic_DNA.
DR EMBL; AB027872; BAA87176.1; -; Genomic_DNA.
DR PIR; T38459; T38459.
DR RefSeq; XP_001713105.1; XM_001713053.2.
DR AlphaFoldDB; Q10172; -.
DR SMR; Q10172; -.
DR BioGRID; 858093; 9.
DR STRING; 4896.SPAC25G10.09c.1; -.
DR iPTMnet; Q10172; -.
DR MaxQB; Q10172; -.
DR PaxDb; Q10172; -.
DR PRIDE; Q10172; -.
DR EnsemblFungi; SPAC25G10.09c.1; SPAC25G10.09c.1:pep; SPAC25G10.09c.
DR PomBase; SPAC25G10.09c; pan1.
DR VEuPathDB; FungiDB:SPAC25G10.09c; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_240362_0_0_1; -.
DR InParanoid; Q10172; -.
DR OMA; PQRTGMQ; -.
DR PhylomeDB; Q10172; -.
DR Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR PRO; PR:Q10172; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005938; C:cell cortex; HDA:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; ISO:PomBase.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR CDD; cd00052; EH; 2.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF08226; DUF1720; 6.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00027; EH; 2.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1794
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000116609"
FT DOMAIN 281..369
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 313..348
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 821..910
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 854..889
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1748..1765
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 651..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1151
FT /evidence="ECO:0000255"
FT COMPBIAS 925..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1406
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1414
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 127
FT /note="P -> L (in Ref. 2; BAA87176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1794 AA; 193279 MW; 1F042BA5E80E9E27 CRC64;
MSYPNQMNGS MYGYGANNGV QPGFDSYGMP INQGGMNYQQ QTYPYQQPYQ PDGYAGNTML
PFQQSQPATQ FNNGFGYASQ PTGSVADYGQ QQQQMYGYNG MMPQTMNNTG FMQPQQTGAI
PGFAPQPTGF VQPQPTGFMS QQPASFMQPQ RTGGAGFIQP QRTGAMPAYQ PQMNNFMQPQ
KTGGFAPQAT GFMQTQPFGA APSFAPQPTG FVQPQQTGVV MPPQPTGYLQ AQPTGPFASF
VQPQQTASFM PAAQPLKPQK TGQIHNSKAM DTRLSFVSAA DQAKFEQLFK SAVGREEAMS
SEIGKAILVR SKLPTVQLSK IWRLSDTTRS GRLLFPQFVL AMYLCNLGLT GKPIPDKVPD
GILNEVNAMV DAISFSLDEN YAKPTQPIPQ AAAQQMAAQM FGGFQQAAGI PSQITGFQPQ
AMMPQRTGMQ PQMTGFQQPM IPQRTGMQPQ MTGFQQPMMP QRTGLQPQMT GFQQPMVPQR
TGMQPQMTGF QQPMMPQRTG LQPQMTGFQQ PMVPQRTGMQ PMMPGLQQPM APQRTGMQPM
MPQRTGMQPQ MTGFQQPMAP QRTGMQPMMP QRTGMQPQMP GMQQPMAPQR TGMQPMMPQR
TGMQQPMAPQ RTGMQPMMPQ RTGMQPQMPG MQQPMAPQRT GMQPMMPQRT GMQPQMPGMQ
QPMAPQRTGM QPMAPQRTGM QPMMPQRTGM QPQMPGMQQP MAPQRTGMQP MMPQRTGMQP
QMPGMQQPMA PQRTGMQPMA PQRTGMQPQM TGGPMLPQRT GGMAPQPTGM PGQWGFINTP
LSNLPGIEAL GQQMMPNAPS GGLNNTFQQK KDIPWAISKE EKRIYDQIFD AWDKERKGTL
GGNAVLEIFG QSKLTRTELE HIWNLCDHGD KGSLDRDEFA VALHLIYRKL NGNEVPAVLP
PELIPPSTRN FTESLNQVKN LIKNDTSNRK PFGAENQSKL KKNSFYDNPS ETTEKDATLY
RHNDSDASAY VSSARRRDFK EEKIESAPPI INDIDSEIAS LKKRIHEKSL VVNALEDKKL
AATPANDVQN DSLIYRIKSV QDEINRLSTS NKSPEVASMN VRLEELSTRV SKMLSDINEV
DHTIASLSLK LFQAEDTKNS YDQTSPEATQ ERNRTISSKL AEMEKQKNES KAALEQMKNY
VTNIENNIRA KLLPSAANDD AWLSQNVVDE SVTRVVKELP VPAPAAPQTL NPPSVSTVQQ
SKPIESNTHT PEVKATSESP SASSNLEDRA ARIKAEAQRR MNERLAALGI KPRQKGTPSP
APVNSATSTP VAAPTAQQIQ PGKQASAVSS NVPAVSASIS TPPAVVPTVQ HPQPTKQIPT
AAVKDPSTTS TSFNTAPIPQ QAPLENQFSK MSLEPPVRPA VPTSPKPQIP DSSNVHAPPP
PVQPMNAMPS HNAVNARPSA PERRDSFGSV SSGSNVSSIE DETSTMPLKA SQPTNPGAPS
NHAPQVVPPA PMHAVAPVQP KAPGMVTNAP APSSAPAPPA PVSQLPPAVP NVPVPSMIPS
VAQQPPSSVA PATAPSSTLP PSQSSFAHVP SPAPPAPQHP SAAALSSAPA DNSMPHRSSP
YAPQEPVQKP QAINNIAPAT NLGTSQSFSP RMGPVNNSGS PLAMNAAGQP SLAVPAVPSA
PSNHFNPFAK MQPPAPSPLQ PSGHDSDNWS QHGDEEEEDS EDDIRSSKDA AALAAKLFGG
MAPAHPVSTP PVRPQSAAPP QMSAPTPPPP PMSVPPPPSA PPMPAGPPSA PPPPLPASSA
PSVPNPGDRS ALLQQIHTGT RLKKTVTTDK SKPIAGRVLD ASDGNSSAWY GNLS
