PAN1_NEUCR
ID PAN1_NEUCR Reviewed; 1533 AA.
AC Q7SAT8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan-1;
GN Name=pan-1; ORFNames=NCU06171;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002238; EAA33504.1; -; Genomic_DNA.
DR RefSeq; XP_962740.1; XM_957647.2.
DR AlphaFoldDB; Q7SAT8; -.
DR SMR; Q7SAT8; -.
DR STRING; 5141.EFNCRP00000005956; -.
DR PRIDE; Q7SAT8; -.
DR EnsemblFungi; EAA33504; EAA33504; NCU06171.
DR GeneID; 3878888; -.
DR KEGG; ncr:NCU06171; -.
DR VEuPathDB; FungiDB:NCU06171; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR InParanoid; Q7SAT8; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
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; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
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..1533
FT /note="Actin cytoskeleton-regulatory complex protein pan-1"
FT /id="PRO_0000349481"
FT DOMAIN 244..333
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 277..312
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 513..602
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 546..581
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1500..1517
FT /note="WH2"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 690..890
FT /evidence="ECO:0000255"
FT COILED 1026..1209
FT /evidence="ECO:0000255"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 164771 MW; C522F302329A6B07 CRC64;
MYSNSNAFLG GANSLRPGQQ PQQQQQQYGA PSPFGQQGPM QPQPTGFAPQ PTGFAPQPTG
FGQQQTGYGQ QQQQPLQQQF TGYPGLQAPQ QQPQLQQQFT GFQPQATGFQ PQVTGFQPQA
TGFQPQAPQQ QPFQTGMPPV PAIPQQFQQQ QSFQQQQQQQ QQPSIQQPQP TGFPSVQIQA
PAQQPAPTAQ GGIAPPPPVK PQATGFSEMA ASFQTAGGKG RRAEQKTNTV KIPNIRLSFI
TAHDQARFET LFKSAVGEGQ TTMSGEKARD LLLRSKLDGD SLSQIWTLAD TTRSGQLHFP
EFALAMYLCN LKITGKALPS VLPDHIKNEV SSMVDIINFS ITDDAGSSSA PASNAPSFAT
QQNTAAVPTI QQPQPQPSNS AILQAQMTGF PAQQTGFMGQ NQGLQPQQTG FPGMNPQPTG
YAGPMPPMPP MPTGFGSNLS PNAGPGGMVA PLNSQPTGMP GQWGLVNTPA TGLPLIDALQ
ARMMPQLGRE QRNYTTAGLQ GNAVIPWAIT KDEKTRYDAL FRAWDGLNKG FIAGDAAIEI
FGQSGLDKPD LERIWTLADN GNKGRLDLDE FAVAMHLIYR KLNGYPIPNQ LPPELVPPSA
RNLSASIGMV KNMLHQESEL RKNTGASLLP QKTGVSYLKG HSFKNTGANR KDATVFKNND
EEVGYRSSAR RRVGTSPRPE SPAASNSGDD LTIEQLRKKI KEKQVLLDAM DFNDEKNMEE
DDILDRRDRR EADELYRRIR RIQEDIDNHP DAQLMSADSD AERRALKRQL QQLTDRIPEL
ASQVRKTEKA IADARLELFR LKDAKAHPNS AAAIVGTGPG GMVTESDRIK ARAKAMMQQR
TAALMGKKID IGDDDADGPK RLEEENIKIK TEKENNERMV RDVEDSVREF AKGIEDSLKE
GAPDSTSEHE KRRWEDALGV EDEVRDFIFD LQRESRAARI RSQDRQGGRK ATQEPVKAEA
PVSTRVETPS PSISRTSTPA STAGGGSYSS YKTPEERAAF IKQQAEQRMA ERLAALGLKA
PGKPGETAAQ RAERERAERA EKRRQAEEED ARREAERQAK LAEEEGGPAP VASPKADSRP
PPPPPSRKAG KADDRRDEEA AAKKAEEERL EREREEQERE TRELEESAKA QEDELAKERA
EADARLKALE EQVRLGKLKK EEEKRKKKAA MAEAKEKEAQ LAARRAEIEA ARKREEELRK
QLEAIDDEDS SSSDEEGPEQ ITPQASTPTV GGSQVGTHEQ EPNSPPPPAP ASVASPPQIV
TTSPNAERES RNPYFKMMSQ SSEASTSSVA APVASPPPPA DVSTNPFHRM TQAAAAPAAA
VSSAVSGAVS GISDAISGVM PSRRRPNDDD DDDWGSEKGS DDEDSDDEGR PGGNSAAALA
SILFGTMAPP RPLSATGEKP TASTPPVVSS PSSPPPPPAP VEPSAGSPPP PPPPPPGPPP
APSGGAPPPP PPPPPMPESG APAAPPPPPP PGPPPAPGAV PPPPPPPPGG APAPSLPAGR
PAGLLGEIQA GRALKKTQTK DKSQAAVAGR VLD
