PAN1_YEAS7
ID PAN1_YEAS7 Reviewed; 1460 AA.
AC A6ZVS5; A6ZVS4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
DE AltName: Full=Mitochondrial distribution of proteins protein 3;
GN Name=PAN1; Synonyms=DIM2, MDP3, MIP3; ORFNames=SCY_2791;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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|UniProtKB:P32521}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000250|UniProtKB:P32521}.
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 -!- PTM: Phosphorylated by PRK1 on threonine residues in the L-x-x-Q-x-T-G
CC motif of repeats 1-6 to 1-15 (By similarity). Phosphorylated by ARK1
CC (By similarity). {ECO:0000250|UniProtKB:P32521}.
CC -!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN61499.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EDN61500.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDN61500.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AAFW02000124; EDN61499.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AAFW02000124; EDN61500.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A6ZVS5; -.
DR SMR; A6ZVS5; -.
DR PRIDE; A6ZVS5; -.
DR EnsemblFungi; EDN61499; EDN61499; SCY_2790.
DR EnsemblFungi; EDN61500; EDN61500; SCY_2791.
DR HOGENOM; CLU_349229_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 2.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF08226; DUF1720; 2.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50031; EH; 2.
PE 3: Inferred from homology;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Repeat.
FT CHAIN 1..1460
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349488"
FT REPEAT 142..153
FT /note="1-1"
FT REPEAT 164..175
FT /note="1-2"
FT REPEAT 188..199
FT /note="1-3"
FT REPEAT 215..226
FT /note="1-4"
FT REPEAT 235..246
FT /note="1-5"
FT DOMAIN 269..304
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 270..359
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 306..338
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 328..350
FT /note="2-1"
FT REPEAT 392..403
FT /note="1-6"
FT REPEAT 409..420
FT /note="1-7"
FT REPEAT 422..433
FT /note="1-8"
FT REPEAT 446..457
FT /note="1-9"
FT REPEAT 467..478
FT /note="1-10"
FT REPEAT 491..502
FT /note="1-11"
FT REPEAT 503..511
FT /note="1-12"
FT REPEAT 531..541
FT /note="1-13"
FT REPEAT 542..549
FT /note="1-14"
FT REPEAT 557..568
FT /note="1-15"
FT DOMAIN 593..681
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 625..660
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 650..672
FT /note="2-2"
FT REPEAT 1076..1081
FT /note="3-1"
FT REPEAT 1082..1087
FT /note="3-2"
FT REPEAT 1088..1093
FT /note="3-3"
FT REPEAT 1094..1099
FT /note="3-4"
FT REPEAT 1100..1105
FT /note="3-5"
FT REPEAT 1295..1300
FT /note="4-1"
FT REPEAT 1301..1306
FT /note="4-2"
FT REPEAT 1307..1312
FT /note="4-3"
FT REPEAT 1320..1325
FT /note="4-4"
FT REPEAT 1326..1330
FT /note="4-5"
FT REPEAT 1335..1340
FT /note="4-6"
FT REPEAT 1341..1346
FT /note="4-7"
FT REPEAT 1352..1357
FT /note="4-8"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..568
FT /note="15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-
FT [PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-
FT [ASQPN]"
FT REGION 185..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..672
FT /note="2 X 23 AA repeats of F-A-L-[AG]-M-H-L-[IV]-[NY]-
FT [DG]-[VK]-L-[QN]-G-[DK]-[TP]-I-P-[YN]-[EV]-L-[DP]-S"
FT REGION 729..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1105
FT /note="5 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V"
FT REGION 1149..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1357
FT /note="8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-
FT [VAS]"
FT COILED 1111..1170
FT /evidence="ECO:0000255"
FT COMPBIAS 1..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 638
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 640
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 985
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 987
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 1230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
FT MOD_RES 1301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32521"
SQ SEQUENCE 1460 AA; 158255 MW; D500EC163DCFC579 CRC64;
MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA FNQPQATGIG
GMPQSFGNSF STMPQQPQTG YNNNGNNGSV YGNGNFGQQP QQQQQQVKPQ HTGYVPNSSM
PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY YQSANTANVH SVQPLQSQGT GYYVSTPNLI
SSNQTQQPLQ AQGTGYYQSQ PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA
TGFVNSFANN GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR
SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS KTKNEVSSFI
DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY MPQTSFGIPL QSQITGGGVA
SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ ITGGAPASMQ PNITGNALQP QTTGMMPQTT
GMMPQTSFGV NLGPQLTGGA LQSQYTGGYG SVMPQQSGPA SMPNLSFNQQ GLQSQLTGLQ
PQPTGFLPPS NFSATMPLTA QKTGFGNNEI YTKSNFGNNL IDNSSQDKIS TEEKSLFYKF
LKLLILKTKV VRFPHCCGNF RKSGLNRADL EQIWNLCDIN NTGQLNKQEF ALGMHLVYGK
LNGKPIPNVL PSSLIPSSTK LLDNLKNQLK TEPTTTKEKP SFGKIDALSY KNNDDDVLPN
YRNRRKVYSA KNEEQSSFSS PSAKSVNHSS STLQTDDISV DKTVEKKTAK PKYSGFSREI
NLKNIASLEN EIKNISNPEN CYDNSIPSDL TSRFDAIIAK LPNLFNEIST IDNEITNAKI
QLYRKKNPSS IIGSGPNGEI TENDRKKAKS RALLRARMSA LTGKSTESED SLSMEDEQQS
AEIKRIQQEN GKNQEIIKDI RSSISDISAS LKSTMTGSNM ISNQEFERWE FGIGLEDGVR
EFLDDLKSNS NKSVTESSPF VPSSTPTPVD DRSSSPSYSQ FKTAEERAAY LKEQAKKRMK
EKLAKFDKNR RNVTQSSRSI SSENSREQPQ QIAGSSNLVE PRATPFQEEK YVEVAQPTQP
VQSTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE DDEEKRLQEE LKRLKLKKKA
DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA APVAPSAAFS QNSTNAPRSV
HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS ASSTSTFDAR AAEMQRRIQR GLDEDEDDGW
SDEDESNNRV AVDNKVEEAK IGHPDHARAP PVTAAPLPSV TPVPPAVPVP QANTSNEKSS
PIPIAPIPPS VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI ATAVQKSGSS TPALAGGVLP
PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD VLSIPESVGT DEEEEGAQPV
STAGIPSIPP AGIPPPPPLP
