PAN1_CHAGB
ID PAN1_CHAGB Reviewed; 1450 AA.
AC Q2H922;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
GN Name=PAN1; ORFNames=CHGG_03282;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ91347.1; -; Genomic_DNA.
DR RefSeq; XP_001229798.1; XM_001229797.1.
DR AlphaFoldDB; Q2H922; -.
DR SMR; Q2H922; -.
DR STRING; 38033.XP_001229798.1; -.
DR PRIDE; Q2H922; -.
DR EnsemblFungi; EAQ91347; EAQ91347; CHGG_03282.
DR GeneID; 4388769; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_001963_1_0_1; -.
DR InParanoid; Q2H922; -.
DR OMA; PQRTGMQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000001056; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 2.
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; PF12763; EF-hand_4; 2.
DR Pfam; PF02205; WH2; 1.
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.
DR PROSITE; PS51082; WH2; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Endosome; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1450
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000349473"
FT DOMAIN 181..270
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 214..249
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 444..533
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 477..512
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1417..1434
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 622..741
FT /evidence="ECO:0000255"
FT COILED 960..1148
FT /evidence="ECO:0000255"
FT COMPBIAS 22..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1450 AA; 156153 MW; 3DED22D7C3BA3DD9 CRC64;
MYSNPNNFFG GNAMGPGAPQ YGAGQPQQQQ QQQQQPDPFA PQPTGFAQAP LQQQYTGYPG
LQAPQGQLQP QFTGYGQTPQ QGMATGAPPM PAIPQQYQQQ FQQQQTQQQQ PQQQQMPFAA
APPQPTQTLA PPPPVKPQAT GFSEMAASFH AGGGARSQPS AAPRKANTVP NIRLSFITAP
DQAKFETLFK SAVGDGQTTM SGEKARDLLL RSRLDGDSLS HIWTLADTTR SGQLHFPEFA
LAMYLCNLKL TGKSLPPSLP DNIKNEVSSM VDIINFSIAE ESGSASATST NAPDFGVRQN
TATPPVIQHP QPQPSSSQLL QAQMTGFPAQ QTGFMGQGLQ PQQTGMPQAT GYTGPRPPMP
PMPTGFGSNL SPNVGPGGMI APLNAQPTGR PGQWGLVNTP ATGLPNIDAL QARMMPQQGR
EQQDYTTAGL QGNAVIPWAI TKDEKTRYDA LFRAWDGLNK GYIGGDQAIE IFGQSGLEKP
DLERAWTLAD HGNKGRLDLD EFAVAMHLIY RKLNGYPIPN QLPPELVPPS TRNFNESLGT
IKNMLHKESD FRKNSGASLL PQKTGVSYLK NHSFRGTGGA SGNRKDATVF KNNDDAVGYR
SSARRRVGNA SPRPESPASV GSNEELSLDQ LRKKIKEKQV LLDAMDFADE KNMEEDDILD
RRDRREAEEL YRRIRRIQED IDNHPDASPI GGDSEAERRA LKRQLQNLTD KIPELASQVR
KTEKAIADAR LELFRLKDAK AHPGSAAAIV GTGPGGAITE SDRLKARAKA MMQQRTAALT
GKKIDVTSDQ DAEKRLEEES IKARTEKENN ERMVRDVEDS VRDFAKGIED NLKEGGQDST
TEHEKRRWED ALGVEDEVRD FIYDLQRSSR ASRIRSQDRQ GGRKATQEPV SAEAPPTARV
DSPASISRTA SPAAPPAAGG SYSSYKTPEE RAAFIKQQAE QRMAERLAAL GIKAPTKPGE
TAAQRAEREQ AERAAKLRQA EEEDARRETE RQARLAEEQG VPPPAVSQAA KPEGKKPPPP
PSRKAAKPDD RRAEEELATK KAEEERLERE RGEQERATRE LESQAKAQED ELAKEREEAD
ARLRALEEQV RQGKLKKEEE KRKKKAALAE AKEKEAQLAQ RRAEIEAARK REEELRRQLE
AMDDDSSSDD EGPEQITPQA STPTMNDSHI VNREPERQPT PPPAPVVSPP QIVTSSPPTE
GESRNPYFRM MSHSSDASPA TAPAPPVAPP VAPPAPPQPE ASTNPFHRIA QAPAPETSPV
PVTRRRPDDD GWGSDKDEED EESDDDRPGG KSAAALASIL FGTMAPPRPL SATGDKSATS
PTVSSPVAPP PESASPPAAS PSAPPPPPPM PGSFPSASPG PGAPPPPPPP PPPMPSAGGP
PGAPPAPPPP PPGMAPPAPP PPPPAGGPPA AAPAGGRPAG LLGQIQAGKA LKKTTTRDKS
AAAVAGRVLD
