ID A0A8S3X5N9_PARAO Unreviewed; 3683 AA.
AC A0A8S3X5N9;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=(apollo) hypothetical protein {ECO:0000313|EMBL:CAG5003303.1};
GN ORFNames=PAPOLLO_LOCUS14217 {ECO:0000313|EMBL:CAG5003303.1};
OS Parnassius apollo (Apollo butterfly) (Papilio apollo).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Parnassiinae; Parnassini; Parnassius; Parnassius.
OX NCBI_TaxID=110799 {ECO:0000313|EMBL:CAG5003303.1, ECO:0000313|Proteomes:UP000691718};
RN [1] {ECO:0000313|EMBL:CAG5003303.1}
RP NUCLEOTIDE SEQUENCE.
RA Tunstrom K.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG5003303.1}.
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DR EMBL; CAJQZP010000963; CAG5003303.1; -; Genomic_DNA.
DR OrthoDB; 10011303at2759; -.
DR Proteomes; UP000691718; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-ARBA.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:TreeGrafter.
DR GO; GO:0061564; P:axon development; IEA:UniProtKB-ARBA.
DR GO; GO:0071711; P:basement membrane organization; IEA:UniProtKB-ARBA.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR GO; GO:0009888; P:tissue development; IEA:TreeGrafter.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR CDD; cd00055; EGF_Lam; 20.
DR CDD; cd00110; LamG; 5.
DR FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1.
DR FunFam; 2.10.25.10:FF:000106; Heparan sulfate proteoglycan 2; 1.
DR FunFam; 2.10.25.10:FF:000074; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000083; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000090; laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000388; Laminin subunit alpha; 1.
DR FunFam; 2.10.25.10:FF:000069; Laminin subunit alpha 1; 1.
DR FunFam; 2.10.25.10:FF:000082; Laminin subunit alpha 1; 2.
DR FunFam; 2.10.25.10:FF:000034; Laminin subunit alpha 3; 1.
DR FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000407; Laminin subunit alpha-3; 1.
DR FunFam; 2.60.120.260:FF:000092; Laminin subunit alpha-3; 1.
DR FunFam; 2.10.25.10:FF:000135; Laminin subunit beta 4; 1.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR050440; Laminin/Netrin_ECM.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR PANTHER; PTHR10574:SF406; LAMININ SUBUNIT ALPHA 5; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; EGF_laminin; 20.
DR Pfam; PF24973; EGF_LMN_ATRN; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF02210; Laminin_G_2; 5.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SMART; SM00208; TNFR; 5.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 15.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000691718};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..3683
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035796661"
FT DOMAIN 16..263
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 394..438
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 439..483
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 484..529
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 530..580
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 581..625
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 626..670
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 726..778
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1377..1422
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1423..1466
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1467..1514
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1515..1565
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1586..1770
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1804..1853
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1912..1964
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1965..2011
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2012..2058
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2666..2869
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2874..3042
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3046..3217
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3324..3497
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3504..3680
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 2380..2442
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2593..2659
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 414..423
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 439..451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 441..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 460..469
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 484..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 486..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 505..514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 530..542
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 532..549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 551..560
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 581..593
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 601..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 626..638
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 646..655
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 749..758
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1377..1389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1379..1396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1398..1407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1439..1448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1490..1499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1515..1527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1517..1534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1536..1545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1823..1832
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1936..1945
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1948..1962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1984..1993
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2032..2041
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 3190..3217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 3653..3680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3683 AA; 405934 MW; 90C17DC95E35201B CRC64;
MGRAVVLLLL YLSAACAEIL TPPYFNLAFG KKITATATCG DEGPELYCKL AGANADHDEH
VIQGQVCDIC DANNEAKKHP PEYAVDSMET WWQSPPLSRG MKYNEVNLTI DLGQEFHVAY
VFVQMGNSPR PGLWTLEKST DYGKTFKAWQ YFSESPQDCE RYFGKESLQP ITRDDSVICS
TEYSKIVPLE GGEIPISLLN YRPSSNKYFD SPVLQEWTRA TNVRLRLLRT KNLLGHLMSV
ARQDPTVTRR YFYSIKDISI GGRCMCNGHA DTCDPADPQS NTNILVCRCQ HNTCGPQCAA
CCPGFEQKKW RISQNWNRFA CEPCNCHNHT TECVYDTEID EKRLSLDIHG NYEGGGVCQN
CQHNTEGINC NKCKPTYFRP YGKRWDEIDV CQPCNCDLHY STGNCEEETG RCECRPEFNP
PNCDSCAYGY FDYPNCKPCT CNLNGTEGDN CTPTDGLCPC KYNYAGKSCE ICEDGYYSPE
CKNCECNSVG SVSHVCDKET GNCTCKSKYS GRTCNQCEAG YYNYPTCKHC NCDTSGTEPS
ICDDVNGQCI CKTGFGGTRC DQCISGYYME VQGRERLCVP CNCSPTGSTS TSCSADGKCN
CLSNFGGKQC DQCSPGYYKY PECLPCNCDL AGSIGSTCDD SGLCHCKPNF DDAKCDKCKA
QFYNYPACEE CNCDPRGVIA TFAGCGSVPA GELCQCKDRV QGRICNDCKA LFWNLQDYNP
LGCEECNCFL AGTLGGLGTC DTRSGQCTCK MNVGGQQCDQ CQGGFYKLET NNLFGCTECD
CDIGGSIDNN CDKQTGQCRC HSRIEGRRCD RPIRAHYFPT LHQFQYEVEE GLTQSGPVRY
RDSEEVFPGY SWKGYVVFSV LQNEVINVVH ISKSSLYRMV LKYANPLRDP VVATIIITPE
SVVDTQQMFN AYLRPTEQPQ LVTVTLEKGN APAPFVMNAG VWTVTIKTTR EVMIDYFVLI
PEAYYEATVL TKLVDKPCVI GERNLCRHFA YPSLSGLPTA DVSTLAVNVS EYITAAEQLR
EYNVGPNDIP LLKNDQSELQ FNMKIHPNGP YVLVLEYVTP VNTTGFVGGA ELEPYNGTQE
NIPRGIITIR FQSGDASESS AVVNINACPY TAACRQVITD DLSKVFIVNV MDANNVISLE
SDTDTIAGIK SIVAVPESDW HLDYITPRPY CLRRDGKCSP GVFSAAVDSK KVEIETGSGG
IRDTRPAGMD NSTVVVYLGP GSEPIKVDSK IPSPGDYLFV IHYYQPDNPQ SNVEITVTTD
DQKYDASLPI EHCPSHSGCR ALITLANGNT QFSLNENFTL LIQGNASKGV WLDYVLVIAK
PDYMDTAVKE ANTLDYTREF IEKCAMNHYH INPNETGFCR DAMFSITAEY NSGALRCLCD
FMGSTELECN TFGGQCPCKP NVIGRTCSAC KTGFYGFPNC KPCNCPLTAI CDDNGQCICP
KNVEGDNCDR CKPYTFNFDV QRGCDDCNCN PLGVVGHQLQ CEADSGNCDC KENVIGRTCD
HCVPGHYAFP ECLQCTCNLD GTTEDVCDQN TAQCYCKKHV RGQACDTCKD EYFNLQPDNS
DGCTKCYCFG KTTRCASSYL TWAEISGMSD WYLVNIEVNR TLNIYPHTIA PSILNDTVIG
AELVSSDEHD QKVVYFGAPE YYLGQRLTSY GGYLSYTIFY TTRDEGYAVI EADVIIGGVN
GYIVYNSVEQ PPSLVNWRHS VRITEDEFTN LDGSAVTRDQ FMNVLVNVTS IYIRATYWHE
AVTTRLVGVS LDVAVEEYTN DGRQASSVEE CQCPKAYRGL SCEQCAEGYY RLSSGPHAGF
CVPCQCNGHS TSCDVNTGIC LECTDYTMGD HCELCIPGYH GDATVGTPHD CLICACPMPY
PSNNFAIGCD LSQNGSLISC VCKPGYGGAR CEYCAAGYYG VPEDIGDYCK PCNCSGNINV
EDPSSCDSIT GDCLKCVNNT AGAACNLCAP GFFGDAIFSK NCTACVCDEF GMERCDPTTG
TCVCRPGVIG EKCDRCAPDH WGLMTGQGCT PCDCALASES SQCDDNTGQC RCAKGVTGKH
CDQCAAGYWN YTKYGCDHCN CNTGYSLGFM CNATGQCECL PGVIGEKCDR CPERWVLIPH
EGCLECDSCT DALIFSIQDL SYLLSNESLE FRDKADSFFT TQRLNYISNQ TERLKPRVTE
LRNVDLDEVT SAVKSLETSS KNLLRSAEFA ATDSDHQITR AAYLAADADK VFESVRDHTQ
KAKDVVTYVS DLATGLELSQ QPKVDSALEE ARQIRRDISA KDLTPKKQQA IGAMNNATKQ
IERMNVFVQP VNEQTKKFQK LVNTTREIRE KLEEMLAYTD LAQHTADAAK TLNDKNRKSK
FGNKVLSVTK LNSAAMKDLI DAALDINNAT FFNTLAAGTV NSSSNSLEDI TTKNQEMEDR
LALLAESLPE LNNLTDVALH HARGLRNRAD SLRALAEREN NNTRTQHAYS AASAYSSIVQ
EISDAKKAAE EADTSVQNAT NINNILYENV TPAKDTSQNL SERALKAQQT VEQKLRPNLT
QAEQALKNAW ATLGAADDED NAIQLSLPTT APSSLESETQ RAANVSATIN YTTDIMSELG
SDLAASKEWA QSLPKLANDA QKMTSNIENL INNIGEMEPK ISSQYRVVKM KQESLEQHRK
EADDKLQKLR ELVEQARTVV NRVPIGVTFD RWSTLQPRLP ETVDEMSTST HVSAYFRTKE
NNGFLLYLGN PKDTMLRRTK SDDFMVIGIQ NGYPYLVMDI GDVAESGLEP ARIGSEKFVA
DNKWYQVIVD RVGRNVKLSI RESLDNGTDY IHSKEATLPG QHTIFNLDRQ KSKLYVGGVP
SDATLQGVSF PAFEGQIEEL MIGDTPVGLW NFVSAANLKG SRQRDKLITS QSGPQEFRFN
GRSHVTMPGR GYLVPQKNHV LLFFRTYAPD GLIYLVGEGN YFFSLQLQDG RIYLQVSLGN
PDDLVIIGTS KTYNDGKWHR LDAGRYLTTC SLKVDGEVLK TVSTSEVKEI PDLDTMNFGG
NNKGIIQVTN KGFDGCIRQI SIDGVNIDLS ENIESVGVAY GCQFASLVSL SGENSYLRYV
NLTTENMLLT LKFKTSKPDG LIFVYLSRTQ TATMSDSISL SLINGKLVLM SQREQLDTGL
STYNDSQWHV VTVIHNNQAL RLVVDDFDYF STDTAPAPLH ILDGVLFVGG VQPSYVVGGK
VGSKTPFEGC IADATINGRV LNLLEPFSNH SVTFGRCGTT TTTGGVPPDK ASWPAPIPAD
VLPTPSPLPP LATPEPEMAT IKGYADENEI FTVPPTEPPT TTLAPFITTT IRPSTTTRQP
PPQPESGCSL AYDPQYGIGD PSEGYRFGTR NDSRIEYSKL PGRQLEGFDF TITFRTFDQH
GGLIFYAEAD KAPGQFLALY MKDARIYFTF NCGGDTAFVE STQMYNGTEW HTVTLVRNEG
HGKLTVDSER IGEASVTCIS PAVLTPPFYY GGLGNITTSV SQNLMDFYQP FKGCLKGLMM
NGQYVTDILY RVNSLRCTDN IEHGVYFGPS NNAHSNYLKL LENFKVGFEI SISMEVKPRN
STGLLLSVHG RRDFMILELL ENEVVANVEN GKGPFHASYK LGNKFSLCDG NWHRIHAVKS
RHVVSVGVDG HFSDAGLGQS GSTDTRSALY IGGHERPIAK VRGVRSRRGF TGCIRNIVIR
ETPIQIPLNA AGRNTHVGVC PTD
//
