PAN1_VANPO
ID PAN1_VANPO Reviewed; 1492 AA.
AC A7TSV7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=Kpol_328p4;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
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; DS480526; EDO14652.1; -; Genomic_DNA.
DR RefSeq; XP_001642510.1; XM_001642460.1.
DR AlphaFoldDB; A7TSV7; -.
DR SMR; A7TSV7; -.
DR STRING; 436907.A7TSV7; -.
DR EnsemblFungi; EDO14652; EDO14652; Kpol_328p4.
DR GeneID; 5542672; -.
DR KEGG; vpo:Kpol_328p4; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_006042_0_0_1; -.
DR InParanoid; A7TSV7; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR PhylomeDB; A7TSV7; -.
DR Proteomes; UP000000267; 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; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF08226; DUF1720; 3.
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; 2.
DR PROSITE; PS50031; EH; 2.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1492
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349486"
FT DOMAIN 321..410
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 354..389
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 661..750
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 694..729
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 982..1022
FT /evidence="ECO:0000255"
FT COILED 1098..1207
FT /evidence="ECO:0000255"
FT COMPBIAS 1123..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1492 AA; 159341 MW; A1B991F0E6246610 CRC64;
MFNSFQQQGT IQPQGTGYYP TQQGQQGQQG QQGQQGQQGQ QGQQQQSFQS QPPFNSYVQQ
PNAGIGGFPQ GQSSFGNTSQ MTNQPSSGFT SGQYAGGSNA NSNLFNQSSQ QFGGVGNNNV
NVNQSSDPSS LLPQGGSYNN AGLQRPQLQP VQSVQSVHSM HSLGPAQTMS SINPIQSQTG
DYYGNALSQQ QSRTSLMSTS SQMGGNQLYD TNSQILQPQQ QQQQQQQNIQ VTAPLQQQST
GLYSSASQPA QAANLQPQQT GFYSQQPLQP QQTGFYAQQS QVPLEPLKPT ATGFVNSFAN
NGINNDIKIP TMRLSFITAQ DQAKFETLFR SRVSKGSNTI SGDNCRAILM KSGLQPKQLA
KIWTLCDTSK AGELLFPEFA LAMHLVNEVL QGDSIPYELD IKSKNEVNSF IDAINMSIVS
GSTEEPAKQA TPFDSLFTNG LSVLQPQATG MIPATSFGVP LQNQMTGGML NPQATGMMPQ
TSFGMPMQVT GGPLLSQTTG GALQPQTTGF MPSTSFGMPL QTQITGGAMM PNLQPQTTGS
MMPNLQPQTT GSMMPNLQPQ TTGSMMPNLQ SQTTGSMMPN LQSQMTGSMG VGTTSFGMQP
QATGNISLQP NPTGFLPVSN FNPTAPLTAQ KTGFGNNEIY SQRNFGSSLG QAEEDSISTE
EKSLFYKIFE TYDSQKKGLL DSPTAVEIFR KSGLNRSDLE HIWNLCDINN RGQLSKQEFA
LGMHLVYRKL NGKILPNRLP PSLIPSSNKI LDNVKNQLKV ASTSNDTKKA PSRTDGLSYK
NNDDENILPS FRNRRKNYST NGTSSSSLDN TPRGSPVTVS GANVSSDTGV TTAVTTSSAP
VAPVASAVVK DGRIDMLQKS IREKRGQLEA EISRNRRMLN QSAENRENDM RMIGSLKDKI
ANVPHILYTK NSSIPDDLNR RIDTIVSRIP VLFSEIADIE FAISNSKIEL YKLQNPSSII
GSGPHGEITD EDRKKARSKA LLKSRMAALT GKAEEAGNSI EEEEARYNKA VANIRNESRK
NRGIIGDIRG SISELSASLM STLTGGAAGQ NTSEFEKWEF GVGLEKEVRT FIETLKSGGI
LSGSSLSTET NLNDKEDERV QYLKDQAQRK MEQKLAELGI NKPAESPSQQ SLSSPSQMEA
QATPVKSPFQ ETQHADERSE DSEDEEEKRL REELERIKLK KKADKEKRLA ELRRQVQDAQ
AESDDGFSSS VSGSNNGNVL APQVEGTVGH VEYPAVPSAA NPVSSVSASM SGSSTPVQGT
SAAARNPFFK STDSSNSTSG LSDLKAAEAQ RRSQRGLDDD ADAWSDDEPS PVAPAPVAPA
PVAPAPVAPA PVAPAPVAPA PVAPAPVAPA PAPVAPSPVA PVPVAPSPVA PAPVAPSPVA
PVPVAPSPAA PQPSNLPPVP IAPPLPQVQG VPQPVVPLAP PLPQVKQEEQ GNFLAPPPSL
PHMDNIQNSQ NLDSHSDQDD VLSIPDSVAS EDELGDEPGL PPSGIPPPPP LP
