PAN1_ASPOR
ID PAN1_ASPOR Reviewed; 1473 AA.
AC Q2UDY8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein pan1;
GN Name=pan1; ORFNames=AO090026000829;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007159; BAE60227.1; -; Genomic_DNA.
DR RefSeq; XP_001822229.1; XM_001822177.1.
DR AlphaFoldDB; Q2UDY8; -.
DR SMR; Q2UDY8; -.
DR STRING; 510516.Q2UDY8; -.
DR PRIDE; Q2UDY8; -.
DR EnsemblFungi; BAE60227; BAE60227; AO090026000829.
DR GeneID; 5994257; -.
DR KEGG; aor:AO090026000829; -.
DR VEuPathDB; FungiDB:AO090026000829; -.
DR HOGENOM; CLU_001963_1_0_1; -.
DR OMA; PQRTGMQ; -.
DR Proteomes; UP000006564; Chromosome 3.
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; 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..1473
FT /note="Actin cytoskeleton-regulatory complex protein pan1"
FT /id="PRO_0000349468"
FT DOMAIN 166..254
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 198..233
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 458..547
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 491..526
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1440..1457
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 678..759
FT /evidence="ECO:0000255"
FT COILED 963..1163
FT /evidence="ECO:0000255"
FT COMPBIAS 298..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 159862 MW; E4ED3DACC85C00E3 CRC64;
MYSSSNSFMG GANSARPGQP PFMQQPSYGQ QTTQQQQQHQ TGLAPQPNGY GSQLSGFGGS
HLQPQPTGFS PGQLQSQMTG FPQLQQQPGF QTSAQPPQLT GYSIQSQAPQ LQVPSSTGLP
VRLAPQTSSE IADSFRGSAG AAPPPPPKTA GSKIPNIRLS FITAQDQAKF EQLFKSAVGD
SQTMSGEKAK DLLLRSRLPG SDLSKIWVLS DTTKSGQLFF PEFALAMYLC NIRITGRGLP
DALPEKIKNE VSSMVDIISF QVPDTQPEMA FPTNAPKFDA PLLENKSAPP APQQPQPQQP
THSQLLTQLT AQPTGFHTQP TGIQSTQASF PGQSSSLVPQ ATAFPGQSQQ QFLQTQPTGL
MSNPQPTGYS GLRPPVPPMP TSLGPNLSPA QTGGVSGLVA QPTGVPGQWG FVNAPSSGLP
NIEALKQQLM PQPGREGGFS AAGLSGNAHI PWAITKEEKK IYDDLFRAWD GFHKGFIGGD
TAIEIMGQSG LDQKDLERIW TLADPHNRGR LNMDEFAVAM HLIYRKLNGY PVPNRLPPEL
VPPSTRNLND SIGTIKSMLS QDAESRKASG AFLQPQKTGV SYLKDHSFRG GSGVSPGFGR
KDATLFKNND EAASGYRSSA RRRVGNNGRT PSPATSQTSE EELSVGQLRK KIRETQIMLD
AVDFQDENRA EEEDALDRRD RREVESLLDR IRRVQDDIDT HPDAAFRNLD NGAERRSLRR
QLQSYEDQVP QVASDVRRVE REIAEAKLEL FRLKDAKAHP NSASNIVGTG PGGAVTEADR
IKARARARMQ ARAAELAGRP TPSSQEDDGA AARRVEAESA KVKADREKND AMTRDVEDSV
KDFARSLEDT LKDASENSTR EHERRRWEDA LGVEDVIRDF IYDLKRNSRT AYVRKEEASR
SMHEEHERSR YDEAPATRPS PPPSTGSTGS LPGSTHEDRV AAARERAQKR IAERMAAAGL
KPHNNTAETL LQRQEREKKE REDRLKQAEE EDTRREQERQ RRLAEEQGGS MAQPAKPASK
KPPPAPPSRR GRTDSAGQAE AKRAAEESAI VEQAAREQTI REEEEAQQER KRLEDDARKR
EEEFQREKEA QEARLRALQE QVQQGKIKKQ EAKRRKEEAD RLAKEQEAKL TVQRAELEMA
KERERQLQLE LEALDEESSS DEEGPENITP QHSTPGQSQI LPEVDIAAPV APSALVPPVP
GPEPDRPTSA TSSPTSDRTG LAHLPLETES KNPYFKKISL PAESQVATPQ PISKAPVTSP
KADVQSTNPF HRLAQQQENA KPAFTAAGPI ERVSRARPEV DDDWSAAGSD FDSSDDDERP
GGGSAKQLAS ILFGTMAPPR PLSAMDDKSP SKPSTPAPDT PVAASTAPEA DGTLSIPSAS
IPPPPPPVVA QVPSIALSSG PPDAPPPPPP PPVPHMAPSA PPPGIPPPPA PPAAPAGAPN
RSALLASIQA GKGLRKVQTN DRSLSSVAGR VLD
