ID A0A194RL10_PAPMA Unreviewed; 1333 AA.
AC A0A194RL10;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=SPARC-related modular calcium-binding protein 2 {ECO:0000313|EMBL:KPJ18015.1};
GN ORFNames=RR48_11863 {ECO:0000313|EMBL:KPJ18015.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ18015.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ18015.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ18015.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ18015.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR EMBL; KQ460045; KPJ18015.1; -; Genomic_DNA.
DR STRING; 76193.A0A194RL10; -.
DR InParanoid; A0A194RL10; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 1.
DR CDD; cd00191; TY; 5.
DR Gene3D; 4.10.75.10; Elafin-like; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 5.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR011061; Hirudin/antistatin.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR028150; Lustrin_cystein.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR12352:SF31; -; 1.
DR PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR Pfam; PF02822; Antistasin; 3.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF14625; Lustrin_cystein; 3.
DR Pfam; PF00086; Thyroglobulin_1; 5.
DR Pfam; PF00095; WAP; 3.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00211; TY; 5.
DR SMART; SM00217; WAP; 3.
DR SMART; SM00289; WR1; 3.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF57262; Leech antihemostatic proteins; 2.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 5.
DR PROSITE; PS51252; ANTISTASIN; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 3.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 5.
DR PROSITE; PS51390; WAP; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1333
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008265287"
FT TRANSMEM 1260..1282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..67
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 68..153
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 153..178
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 270..318
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 320..387
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 531..556
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 590..636
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 638..707
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 829..882
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 920..986
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1077..1133
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 86..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 358..365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 367..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 678..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 687..707
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 957..964
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 966..986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1333 AA; 143130 MW; 4EBF466C452FBF9E CRC64;
MSTRAVRAAL LCACALLLQY ASAELRGRCP AEGGTCPARA APCSVDDDCG EKICCNTACG
RACVDPLYTG CENIKMSSER ISRALQAENS RSGRSAPGVR TPRCRASDGE FEPVQCDNEI
VSACWCVDTA GFEIPGTRAP AASLVNCTQQ ASCAAHTCRM LCPLGFELDQ RGCPLCRCRD
PCAGVTCPSQ LACQLEEIDC LKPPCPPVPT CKRGRSLQNI CPAGEPLLIS ETSRPFLCGT
DPGKPNCPPL YRCLVEPGND YGVCCPASLE LQKAGTCPAV DPSAELECGT PCAHDLECPS
MQKCCDGGEC GRHCSLPHNV TMCTQQKMLA ELLVVSEKEG RGYVPQCGED GAFISKQCSR
NGLVCWCVDS DGNKLRGSMG PSASVHCSPV PRPARTGARS LTACARALCA GVCEYGYKSG
ADGCPSCECD DPCSGYPCSE DEECIRVKDS DCVGELCTGY PVCRPRVSYE NPCAIGTPAT
DQAGSVLNCE VDADCVNGHI CQHTRRSGHA VCCPELAADN STDTENVELS CLELTCRMGC
DYGFELGAER CPTCRCRDPC AGVSCPQGRA CALVDVACDA DYCPPVPACL PRKPGQCPYL
VPATGSCEWA CRADAECGPG QRCCATGCGT ACTAAVHLTA CQHTRALALH TAAEKGSPPS
WTWIPECEED GTYKRIQCKE SEKICWCVDS AGNEIPGTRS TNSTPSCDAP APCPDPGCNQ
EEVCAHGPEL DDRGCPTCVC RDPCADVNCR HDETCELVPL DCDGETCAPL ARCVPAPQCP
EGEPLQAPGG GALLACGPQA ASCPSTHACR FAPHDPQPAV CCPKPRTVCF ESKDEGLCES
GGLNVTRWHF SAARNRCERF TYHGCSGNHN NFRTKEECNA VCPVEEVTSK LTKEKSREII
GQNGGMSIDF LYHPSTCSLL SPCERLREKN EAATQKYGKG SFIPECDAAG GWQPVQCMAH
IDVCWCVSAR GEPQKGSLVR GARPTCNFRQ ARKWMRRDPD DERARADEVL EELIRQMTSY
RVEELEEEDL EDEIDEQSKE STTDSAAVLV SEVVEPRLSQ TTRHDAPVVI SDKIVFKTKC
QVLLEEAEKG NEGVEPRCLS DGSFAPQQCA RGRCWCVDAA GQRRQPQPAT ATCEMTQIES
AILELELVGA SNDEGERARA ALSARLATLG ARVPVSVQRD QHVVRLRVQL AGLRAADMAF
HLENMVKKEK LAGVRKSDSG VLGADVIRSE YRLAVPAPAL QQREIVTEST VSSATSYHTA
LIVLAATSAF IISVLCVLVM LYRARLQREP QKAERFLPQA PPVYVLSANE KAELARALHA
PNNSNEESDS QRV
//
