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Database: UniProt
Entry: A0A6I8U4W6_AEDAE
LinkDB: A0A6I8U4W6_AEDAE
Original site: A0A6I8U4W6_AEDAE 
ID   A0A6I8U4W6_AEDAE        Unreviewed;      1830 AA.
AC   A0A6I8U4W6;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   02-APR-2025, entry version 17.
DE   RecName: Full=Patronin {ECO:0008006|Google:ProtNLM};
GN   Name=5573475 {ECO:0000313|EnsemblMetazoa:AAEL026939-PV};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL026939-PV, ECO:0000313|Proteomes:UP000008820};
RN   [1] {ECO:0000313|EnsemblMetazoa:AAEL026939-PV, ECO:0000313|Proteomes:UP000008820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL026939-PV,
RC   ECO:0000313|Proteomes:UP000008820};
RG   Aedes aegypti Genome Working Group (AGWG);
RA   Matthews B.J.;
RT   "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AAEL026939-PV}
RP   IDENTIFICATION.
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL026939-PV};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000256|PROSITE-
CC       ProRule:PRU00841}.
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00841}.
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DR   EnsemblMetazoa; AAEL026939-RV; AAEL026939-PV; AAEL026939.
DR   OrthoDB; 2125658at2759; -.
DR   Proteomes; UP000008820; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0036449; C:microtubule minus-end; IEA:TreeGrafter.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0051011; F:microtubule minus-end binding; IEA:TreeGrafter.
DR   GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:TreeGrafter.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:TreeGrafter.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR   FunFam; 3.10.20.360:FF:000002; Patronin, isoform M; 1.
DR   Gene3D; 3.10.20.360; CKK domain; 1.
DR   InterPro; IPR032940; CAMSAP.
DR   InterPro; IPR022613; CAMSAP-like_CH_dom.
DR   InterPro; IPR031372; CAMSAP_CC1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR038209; CKK_dom_sf.
DR   InterPro; IPR014797; CKK_domain.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   PANTHER; PTHR21595; PATRONIN; 1.
DR   PANTHER; PTHR21595:SF0; PATRONIN; 1.
DR   Pfam; PF17095; CAMSAP_CC1; 1.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; CAMSAP_CKK; 1.
DR   SMART; SM01051; CAMSAP_CKK; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50346; PRC-barrel domain; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51508; CKK; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW   ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000008820}.
FT   REGION          360..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          993..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1065..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1208..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1388..1418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1462..1491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1528..1682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          802..836
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        370..384
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..431
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1005
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1022
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1028..1050
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1096
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1130..1141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1208..1224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1293
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1393..1417
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1528..1538
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1558..1569
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1576..1587
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1592..1607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1644..1663
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1830 AA;  203685 MW;  8E3535382181D4F6 CRC64;
     MDSQQAPQPR SAYDMETQES RFAKQRASVK WLLSKAYNNR VPEFLKDPFY RDHEGQDHLK
     PQIVVGLGNA SIYCQVLSNI YSDPNYQSLN HWSILQTLSR KGVPLNESPD LPLTETVLIQ
     TNPLRINAHM TVIEALMVLY AKEVASSGRI SSALERISGR SVSQGAQHHE AALLSWISHV
     CSALKRRIDY ELTNGVGGGN GGGGGTNPAV DEYGQRLQSP TIAPVRDFRE LCDGVCLAYL
     ISYYCPKLVP WHSVKFNHVP TIEDSIHNIL IVSNFSERSL PYSVFHMTPE DITYMRGAMK
     QNLVVLLADL FNLFEIHPAK CVCYPGMEQQ QVADSAATNE HGIAHRRGFA THPPILAIPE
     LRSGLDSPPG SGGSAGSGGS GNGGAHPRPP FQVTRSPSAS TLRKHVSTRD MHDQQQPQYS
     QHPQQSHQPY HQDQDEGFVV HRSKGVPTLS SMQEPLVPAR IRQAKEKTNN DSKAEERGDS
     IPAGRPSNWE ENRKQSFSGR RSRRNSLSED SQLTIENFGG SQDQLNTIGR FDRERKTSSA
     SLTSVEPVTP ARSSIADARG SIQFGYDTDS SGNEKQDRDT EKPTPALRRH NSTNLHSSSV
     ERDIIDGDMS ATHGFGGGSG PAGPVSVADV ETTPRRKTSF ATLPNNTTTW QQQAISVQKM
     EDVDDSQSGF EDATKISTIK LKLEEKRRLI EQEKRRMETA WSKQLQTVGK QAFLQAINKQ
     GKGGGSMSES DTSKESPESA TMMMVEDSIT SITTTTNTST TVDRAERPCS LQDLDDQNKY
     ESKWNAQIIE PKKTPDLENM DLEQYQQSIS KMNSNLHDIQ ADIQRLTQQQ TQIQAQTLQA
     QQLLHAQQIA NLLNQQYGSQ QNIQQTIHGT YRPINAQLFG SSPHLPQQNA PLLQQQSPIN
     YGTRPPSRDP YLSQQQQLHT LQYVNDQGQY IQQAQQQQQQ QQQHYMGYEN GQYRKENQYS
     SNPYLNIDQQ QQQFYQDSNH YRDPYLPQEV KEPPIQQSQQ PQHNQFFLHD SSGGGGGGGG
     LGTPPQPAQR RTWAQSAAAA ANQRGSSASS DIQLDINAWN QGIKSSPYNK SPSQSGFSLH
     HNGDSGGDGY GTGSRYGGSQ QSFQNLFEVH HGSSSSPQHS RVRNQISQMI NHGGSSNSSP
     GAETRNSHHD SFRDNRNMPL SPPIDDMAPQ SISFIGDEDT GDIEINTSKG TSFTLRQQHQ
     QDQLEQLYGS SKPGSNKLQH NNGPELNKHL SKLNITSGNR TYRIPSPTRP TLNSNSFHDP
     QQDEVNEKGF YISFDNEQPK RPKPPLRTKR SPKKDKLGDG MEHSKESEKP SHRENNQNNF
     GTFSVKTANS FSANFNEEQV VSRKSIIDSA SSPFETAATG SSRASNNNMA ATMERDIGER
     RHLEDVTNHT STGSNAMNNN NIHHYNNNNG DGYGSENENQ RKAKLVIGND EGNLDPNSVD
     EMERKKEKIM LLSLQRRQQA EEAKARKEIE AMQRREKERE KEEERARKKE EQFARRQAIL
     EAHKLKKAIE EAEREGKTID RELLIKHQQS QAQLHQSSRG GDGGMHHQTS STPAAKMRPQ
     KLSRPRPKTI HVETGSVDLS ETSSLSSRGK KGSNSNLTGI GLHSSNSMRR DYYRGSQDSL
     AIRDSDSGLG RATPPRRAPS PGMGPSSRHL PSPSGPGSLP PGLITKRRGF DDGSSDISST
     ASSMMDYNGP KLYKQPATKS NRGIILNAVE YCVFPGAVNR EAKQKVLEKI ARSEAKHFLV
     LFRDAGCQFR ALYGYWPENE QIIKLYGTGP SQVDDVMFDK FFKYNSGGKC FSQVHTKHLT
     VTIDAFTIHN SLWQGKKANL PSKKDMALVI
//
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