CLOT_PENMO
ID CLOT_PENMO Reviewed; 1670 AA.
AC Q9U572;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Hemolymph clottable protein;
DE Flags: Precursor;
OS Penaeus monodon (Giant tiger prawn).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6687 {ECO:0000312|EMBL:AAF19002.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-76; 129-144; 149-163;
RP 170-185; 230-249; 486-497; 692-711; 781-799; 1259-1278 AND 1637-1656,
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Hemolymph;
RX PubMed=10561606; DOI=10.1046/j.1432-1327.1999.00909.x;
RA Yeh M.-S., Huang C.-J., Leu J.-H., Lee Y.C., Tsai I.-H.;
RT "Molecular cloning and characterization of a hemolymph clottable protein
RT from tiger shrimp (Penaeus monodon).";
RL Eur. J. Biochem. 266:624-633(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 15-44, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Hemolymph;
RX PubMed=9972292; DOI=10.1016/s0305-0491(98)10085-8;
RA Yeh M.-S., Chen Y.-L., Tsai I.-H.;
RT "The hemolymph clottable proteins of tiger shrimp, Penaeus monodon, and
RT related species.";
RL Comp. Biochem. Physiol. 121B:169-176(1998).
CC -!- FUNCTION: Forms stable clots in the presence of calcium.
CC {ECO:0000269|PubMed:9972292}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Also exists as oligomers.
CC {ECO:0000269|PubMed:9972292}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in gill and
CC heart. Not expressed in hemocytes. {ECO:0000269|PubMed:10561606}.
CC -!- PTM: Glycosylated. Contains mannose and N-acetylglucosamine.
CC {ECO:0000269|PubMed:10561606}.
CC -!- PTM: Substrate of transglutaminase.
CC -!- MASS SPECTROMETRY: Mass=380750; Mass_error=800; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9972292};
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DR EMBL; AF089867; AAF19002.1; -; mRNA.
DR AlphaFoldDB; Q9U572; -.
DR SMR; Q9U572; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0042381; P:hemolymph coagulation; IDA:UniProtKB.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemolymph clotting; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000269|PubMed:9972292"
FT CHAIN 15..1670
FT /note="Hemolymph clottable protein"
FT /id="PRO_0000041591"
FT DOMAIN 15..764
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1390..1550
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 15..674
FT /note="Vittelogenin"
FT REGION 198..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1392..1513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1414..1549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 42
FT /note="A -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..76
FT /note="LD -> DL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="H -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1640
FT /note="Q -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1642
FT /note="Q -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1670 AA; 188458 MW; 5280EF8181E6D4AF CRC64;
MKALILLLLG ACQALQPGLE YQYRYSARVA SGIPSINRQF AAAGIQADVT VQMAADYSVV
VQFSNIEVGD LNKVLDCDLR APLPIEYHPL EDYVDLLEKP FRVIMNESHV PSYMEGPEEP
IWISNVRKGF VNIFRVPLFW STELHSTKLN YGAVEETLVG RCQNWYTSMK LPVNLAEEVN
VQREHFMEED IQRDAYSSSY TTKTKSKTSS KTSSKTSSKT SSKTSKTGKT SPGQLANVPH
IEDTLWSVRR TTDFDMCENL VSLQIHSSKY TEDIIQRSSV ASYLIRGDTH RRIEQVVVEG
TITVLTNKEQ HEHVDTFTNQ TLELKAVREV GEPITVTYDV HPHYDWQYDI ERPQGDQFIP
LEQVLTGRPV TDQIVNSIME YIKKTVDDLS HRMEHYPAKP ENLAYIIGRL VEAVANLDYP
YIQTLYTHFD GKGTMQKYIF VQLVIHAGTE PAVNFAVDNL SDILFYVTFY ESIGVSLRTP
APIPKIMHSL INGEEGLHHS LGLMNFATLA HDACLSEDRK HFYFDYSCGP KTTCDPELII
TNFIPYLVRE LGNQGKDVWQ RLIYLQALSN LGTPQTINVL KPIILGVTET NIFMRTNAIW
SLSAYNMHKT ALSQIYEILM PIIENKGEQF EIRNIAFLTL ATWGPGHAWW QQLAVSTWHD
PSPQFANFVT TTIYSISDSH TKLAETVSRI KHLCKPAAPA SILHSTNFFL HEYLFSEEHG
SRVNFAWFAS VHGAIPEEVF LRIQREFFYG YTKVLKIDGQ QRGLYNLMQL MKQKMTKPQK
RPQSSAQEIV SGMWEELKEK IGFTSPESAS DATLWLKLDR LIYVALQYHF MEGAPIPYGM
YSGKPFYDKD LNTLIAFPTE IGIPFSVLYV AEDATWLNIN GNPETSMTSG KMKVNVDFIF
ETSQVQFVDA RAHVPWSKRP AVASGVYADT QLVLPLNVHA SFDMYSQEIQ LSIEPTNTQK
IDVIKFEFIP YTVLENNYPG DVLVIENEYK PILHGEVPLF NDKHQAFPSD VGLWIQVATE
GDIHHTPSIY EIITQLFSAH TSTHIWEQSI VFDPTLSTTK TVSFTFNYVS TGGSGSLVDR
GDYDDGQISQ GSFDEDFGQF SQVAGGSDQD IMEVDSFGTQ SQTIERIMRL QQALISSGGH
VRTISVEVEL QGTPTRNYEA SLTWAISSSA STRSSKVQVT LIKHPAVGVL EDPYTICLNA
QIVKPHFNPF FTTEDVLTAN YHSTVKAELF EGETCEEAPV LLLEASFDVS SNVKERVKEA
IEKGCDYSTY APGIDIITSP LYDHSHITAT WTPDFPDNLK NITYYVDDII KASLSKKIEF
DHTSAHHASR VEIDATKCIE TGLWTVRTEK PYAVSIINEL ELPAWANPIF TPAPLATTLL
YGLTVGRTPV SCTIDETKVR TADGKVFAYE PSECWNAMTL DTTFDQRGAM LVRNTGQWEV
RIIWQKEGLV IDMSPTNFLV NGEPAKGTDN RYTVLHHDDS HTIVFESGTS VKVSDKVEVL
LGLDHRGHTT GICGNFDGEP SNDMVGPKGC YYTDGPLFAL SWASPGEGCA SFMYKNLKRD
VVWYQENCPH FTYEPTGVTH ADALYDCTEW VYHQRTEGQY HCKALSPMPV CRPECVASHP
ITTSVEYECR FSGHQQQAQQ QQQQQVQGTQ WEECFPHFYT LTYPSSCIPQ
