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Database: UniProt
Entry: A0A0N1PEQ6_PAPXU
LinkDB: A0A0N1PEQ6_PAPXU
Original site: A0A0N1PEQ6_PAPXU 
ID   A0A0N1PEQ6_PAPXU        Unreviewed;      4298 AA.
AC   A0A0N1PEQ6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Spectrin beta chain, brain 4 {ECO:0000313|EMBL:KPJ04733.1};
GN   ORFNames=RR46_01222 {ECO:0000313|EMBL:KPJ04733.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ04733.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPJ04733.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ04733.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ04733.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826}.
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DR   EMBL; KQ458863; KPJ04733.1; -; Genomic_DNA.
DR   STRING; 66420.A0A0N1PEQ6; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   CDD; cd21193; CH_beta_spectrin_rpt1; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 16.
DR   Gene3D; 1.20.58.60; -; 24.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 29.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 31.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 24.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 2.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          38..141
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          227..332
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          913..970
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          3861..3969
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          3750..3850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4005..4149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4180..4205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4225..4298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          655..696
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1499..1543
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1589..1649
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2801..2835
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3193..3251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3394..3453
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3599..3626
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        3816..3830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4036..4054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4126..4146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4252..4266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4268..4283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4298 AA;  486254 MW;  DD2B9C6441728E7D CRC64;
     MSVCTPIRIT SRRGDLWPVD ALKFEQGRIK ALQEERLHIQ KKTFTKWVNS FLQKARMEVE
     DLFVDLGDGR RLLKLLEIIS GERLPRPNSG RMRVHKIENV NKSLGFLHTK VRLESIGAED
     IVDGNPRLIL GLIWTIILRF QIQEIEIDVD EENESSEKKS AKDALLLWCQ RKTSGYHGVR
     LESIGAEDIV DGNPRLILGL IWTIILRFQI QEIEIDVDEE NESSEKKSAK DALLLWCQRK
     TSGYHGVHIH NFTDSWRSGL GFNALIHAHR PDLFRWAEVP QADHVETLNH AFDVAHNHLG
     IPRLLDAEDV DTSRPDEKSV MTYVASYYHT FARMKNEQKS GRRIANIIGQ MMDCDSRKGE
     YGRLMSALLE WIRLKILELN GRELPNSLDG IQRLLLAFKQ YRTVEKPPKY KERSEVEALY
     FHINTMQKSL VGEAWAPNEG HLPQDLERAW QKLEQAEHAR ELALRTELLR QQRLEQLNYK
     FNTKSVLRKG YLKEMIQVLS DPRYGSNLAQ VDATVKKHEA ISADILARTE RFEDLSAMAG
     ELVREQYHGA EAVSRTEQAV LARWRELLEL LERHRTSLAR LAHLMALLRE ADAVAHTLLE
     MKAQFQSEEV GRHLVDVERL LQAHALQELQ LGALDESIRR LVRQGAAAEG PPQPTQQLAA
     QLAKLEDACD SLMAAAKDRK ARLEDARNLY QFLEDHDEEE GWVTEKQRIC RAEVAAKDLR
     GVLALRQKHT ALLHELRARD LVAQRHRERG QSLIEAKHPK SAEVERRLAA LSKQWELLRQ
     LAEARDKQLA DAAEAHQFYG DANESESWMK EKRALVGTAD CGRDAAGAGA LLARHRLLHG
     ELQAYEPELQ QLRAAADRLQ SAGIHELQLP TEVEAGPALE EEEWVNETRL VPTEVWEEEP
     VERLEHRTVT EERSVPQVKA LYAFTGQGIS MAKGEVMFLM NKTNPDWWSV RKADRTDGFV
     PANYVREIEP RVVPVQVRRP EKVRTVQRVK KTVLVKQVVP VRRGTTRPAR RASRAQPVAL
     AKAPAVGERM QHIEQQYGEL VKLSEARRLQ LEDAIKLYSF FAECDDFDKW IKEKEKMLRT
     DDPEDSVDTA KRKYEKFVTD LSAASKRLEH IEAAAEELVA AQHGQAARAT ARRQQLRQQW
     ARLLRLKEQK EMHLEGASSV ELFQRTCDEA LEWMCEKEQQ LAGVGGAGGG AGADLRTVRA
     LQRRHAQLER ELEPLREKVN TVALLADSVK SQYPSERGNV EARQQQLQQA WLRCQAQAAE
     RRSRLESAVG LQVFASNSAQ LHDTVQKVRE QLQQEVTAKD VATAEALYKQ HQELHDDIKG
     YDDEFKEVIG LGKQLLANNP SLTDVAEKIK TLEAEQKALH KEWQEKEVVL KQGVQLQTFN
     READQIDASS GAHEAFLEYN QCGSSVDEVE ALLKQQEELE ARLGAQDERL AAFVQRAAAL
     ERQQPRHYAE KHIAARRAAV VQRRDNVRQA AAERRRALLA SLAHQQFVAA ADELQTWILD
     KTRTAKDQSY RDLANLERKL QKHEAFEREL QANEKQLRNV ESIGQSLQKS DPARAEEVSE
     RLRDLQTAWE ELVAASRDKG SKLRQAAQQR QHRRAVEDAK ARLVDLERAL KSEEIGTDLR
     SCKRLLNQHQ ALEQELSQWE SRAKALAAQG EDLVSGGHFD GAAIERDSAA LLAALDKLRP
     RAAARRAALE TSMRLHKFAA EVSGELDWLQ ERQAAASSTA LPSDLHAAQA AQKKHAKLRA
     ELLGRRPLIE RVLAQGRTLV EEEHPQKEKI EELSDELEAA YSRVSAAAEE RGARLEAALR
     AQQFLHEALE VDSWLADKAA ALASADVGAD RHRATQLLTR HKAVELELDT YAAIIAEMGH
     VAASMGQPEL VERHALLAGS LARLQRLAQQ RQGALVESVC RHEYLAESAE LESWIQEQYA
     AASSEDYGQD YEHLLILRSK FEELRHRVES GAERFNQCEE LAKKLLASDS PYIADIERRQ
     EALGESWQRL VEQIGSRAQR LHAAGEIHRF HRDAGELVGR ASERAARLAA PPPPRDLRAA
     TALLRDHDTL ETDLLAIDAQ MQVLQEEVQQ IALRQRALSD AWAALRSAAD QRRLLLHQHL
     ELHQFLSEVR DVLTWSAALR GGMAGAARAR SAAAAQAQRA HHDALRAEID ARDDDFRLAL
     ERAQRLIDAR HPAAQEIAEK CEAVVEERAQ LHSAWAARQV ALDQLHDLHC FLRDAKQLHE
     LCASQEAALS TEISPTCSVE EVDNQLKKHE AFEKLLATQD EKLTTLNNHG DKLLQQNHVE
     SQRIADELQQ INERRKKLYD SAALRREQLV RSRARAQFAR DAAEARAWVA DKLAQLPAQA
     GEVTDLEDKI KKLKKHQAFT AELAAHKARL QEVQALAEQL RPDAEVDRQL QQLQNDWQLL
     ETATEQRGRG LEEAQDMLEF NQHLDKIEAW IRDKEMMVQA HELGRDYEHC SALLRKLDDL
     DSDMKVDDKR VRALVALADK LLQKGGGAGA QAGGVAARRD AVLGRWRALS GALQAYRDRL
     DAALLLHSFN RDVEETAERI SKKAAAFSSE ERGRELPAAE ELRRRHLARW AEARAVADRL
     KALHQEGDRL AASHPESAGE ISSSLHRLDA AWDELQQLAA RRTALLDEAI AEHKFDDTLK
     ELEVWVSETV KRMDSAEPPE SVADAEALLE VHHERKAEID GRQKAIASLQ KEAESAGRPE
     RIQRVATLAD SLDQAWLQRK QYLTQAHELQ LFKEQAQQTE DWLASKEAFL NNDDLGDNLD
     AVETLIRKHA EFAKLVESQV GRVAEVQRFA AGLLQRDHYD AAYIQRRVQH LLDRAQRLKE
     RCDERESKLQ QARQLQEFRR NLAHEREWIE LKMQIANDQS YRELSNLQSK IQKQAAFESE
     LAANKKRIDD VANTGEELIE EKHYASQEIA KHVEDLENLW RELQAAAKLR RERLQEAYQA
     RVYLRGLDDF TAWLDDVEAQ LLSEDHGKDL TSVTALLKRH TRLEQQCASK ADTAAQLADT
     AHQLARNGHF MAEDILERAE RAVTRYKQLQ EPMQIRRDNL EDAALLHRWD RDADEEFDWL
     RERGAELESD APLGDSLPEA QALLKKHLAL EAELLAREPS IKALSGRAST LSRRGHFAGA
     ALERRAAELS QRLRCVVEAA GARACSLRAR ADLLALLAEG AEAAAWLAAR RAPLAAPDVG
     RDEEDVLALT RRLEAQIREL ATFDSTLARL EKTAAQTDRS PADAETVRTM LQELQSAYEE
     LKLLAARRQQ RLQQSLKYFK FVQECSEAQE WIGEQMATAA SEDYGLDVEH VDTLQQAFDN
     FLTQLHANEG RIEAVCEAGG ALLEDNAPEA DRVRQRIDDI RGLWDDLKEL AVARQEALAG
     ARQVHEFDRR AEETGAWIAE KEAALQLHRQ LHQLRALRAD LLAIQDAHKE LKQEAERLGA
     AFPDAREHVS AKLEEVSEAL GALEAHAAHS EQQLALADHL QAYFQTYQDL LAWTNEMIAR
     VTAPELAGDV AGGERLLARH RDMRAEIDAK EDAFHTLYSD GEKLVREGHF MANEIEERVS
     TLRSRQGALE AAWRARATVY ERHLDALIFL RDADSLEHWI LTRMPLVRDG KYGSSVAQTE
     ELINRHRDLE ETIESQKDKF NALKRITLRY RHPFHYLAWR ARATVYERHL DALIFLRDAD
     SLEHWILTRM PLVRDGKYGS SVAQTEELIN RHRDLEETIE SQKDKFNALK RITLIEQAFS
     EQQAEEEAAR RRYAEKQEAE RLQQYRRREM DRIAEERRRD TAPPPQTTPT THTPTAPLQP
     TREVERVVAT GSANTMGPAK AASSEENVSA PLDRPQRTDT HVKRAESMSV VKTPKRTPSF
     TTRRRTQSFR RHRHDMDELP PVEIEGYLER KQEAGCGGVR ATVRSWRTYY AVLCGQLLCF
     FRDQHDFGSA KAAAPPVAIL NARCEAASDY TKRANVFRLS CGDGAEYLFA CASPQLLAEW
     VAKLAFHAHL PPELQLTPYS EASAAATATT TTTTGVTTDE LRRRLHENAS SSSSAASSPE
     PRRAGRSQAE ILQEHRNSQQ EQRNSQKRAS ATPDRHIESA VLPSLPPRQP PAQPPQTSHE
     EPADVVLRNV SERSGSPWGR SRFSNGRDLN AEFLRSQREA ESGAPPLPAS VPPLPDRAPP
     LPDRGPNLPE RVSMIAERGL LDKNPQQSVT ALVNSYQQKM TRSWQEKDQN RNPTWQGQGQ
     GQNNNWQTVE TTSHFYSASE LAYGEGSAGA GAGAGGTRPA SVAGSGGSPA LDQRPASRSS
     GESELSVGGV SKDKKDKKGV FGGLFSRKKR PQSHMYLY
//
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