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Database: UniProt
Entry: P98092
LinkDB: P98092
Original site: P98092 
ID   HMCT_BOMMO              Reviewed;        3133 AA.
AC   P98092;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAY-2019, entry version 116.
DE   RecName: Full=Hemocytin;
DE   AltName: Full=Humoral lectin;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Bombycoidea; Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fuyou X Tokai; TISSUE=Hemocyte;
RX   PubMed=7873598; DOI=10.1016/0167-4781(94)00202-E;
RA   Kotani E., Yamakawa M., Iwamoto S., Tashiro M., Mori H., Sumida M.,
RA   Matsubara F., Taniai K., Kadono-Okuda K., Kato Y., Mori H.;
RT   "Cloning and expression of the gene of hemocytin, an insect humoral
RT   lectin which is homologous with the mammalian von Willebrand factor.";
RL   Biochim. Biophys. Acta 1260:245-258(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2221-3133.
RA   Kotani E., Iwamoto S., Tashiro M., Mori H., Sumida M., Matsubara F.,
RA   Yamakawa M.;
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adhesive protein and relates to hemostasis or
CC       encapsulation of foreign substances for self-defense.
CC   -!- DEVELOPMENTAL STAGE: Expressed in hemocytes during larval-pupal
CC       metamorphosis.
CC   -!- INDUCTION: Hemagglutination activity is increased by bacterial or
CC       viral infection and inhibited by D-mannose, N-acetyl-D-
CC       galactosamine and D-maltose.
CC   -!- PTM: May be converted into the 260 kDa mature hemocytin by
CC       proteolysis.
DR   EMBL; D29738; BAA06160.1; -; mRNA.
DR   EMBL; D14035; BAA03124.1; -; mRNA.
DR   PIR; S52093; S52093.
DR   RefSeq; NP_001104817.1; NM_001111347.1.
DR   SMR; P98092; -.
DR   STRING; 7091.BGIBMGA006692-TA; -.
DR   PRIDE; P98092; -.
DR   GeneID; 692743; -.
DR   KEGG; bmor:692743; -.
DR   eggNOG; ENOG410IR7U; Eukaryota.
DR   eggNOG; ENOG410YF4H; LUCA.
DR   KO; K03900; -.
DR   OrthoDB; 12226at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00057; FA58C; 2.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012111; Hml.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; Unchr_dom_Cys-rich.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF08742; C8; 3.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF01826; TIL; 4.
DR   Pfam; PF00094; VWD; 3.
DR   PIRSF; PIRSF036569; Hml; 1.
DR   SMART; SM00832; C8; 3.
DR   SMART; SM00041; CT; 1.
DR   SMART; SM00231; FA58C; 2.
DR   SMART; SM00214; VWC; 5.
DR   SMART; SM00215; VWC_out; 1.
DR   SMART; SM00216; VWD; 3.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF57567; SSF57567; 4.
DR   PROSITE; PS01185; CTCK_1; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
DR   PROSITE; PS01285; FA58C_1; 2.
DR   PROSITE; PS01286; FA58C_2; 2.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS51233; VWFD; 3.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein;
KW   Lectin; Reference proteome; Repeat; Signal.
FT   SIGNAL        1      ?       {ECO:0000255}.
FT   CHAIN         ?   3133       Hemocytin.
FT                                /FTId=PRO_0000021445.
FT   DOMAIN       40     96       TIL 1.
FT   DOMAIN      153    209       TIL 2.
FT   DOMAIN      248    455       VWFD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN      509    576       TIL 3.
FT   DOMAIN      770    837       TIL 4.
FT   DOMAIN      940   1095       F5/8 type C 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN     1116   1254       F5/8 type C 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN     1619   1824       VWFD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     1890   1948       TIL 5.
FT   DOMAIN     1953   2179       VWFD 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     2229   2285       TIL 6.
FT   DOMAIN     2553   2622       VWFC 1.
FT   DOMAIN     2842   2907       VWFC 2.
FT   DOMAIN     2971   3076       CTCK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00039}.
FT   COMPBIAS    895    914       Poly-Thr.
FT   COMPBIAS   1267   1270       Poly-Glu.
FT   COMPBIAS   1425   1428       Poly-Thr.
FT   COMPBIAS   1447   1450       Poly-Thr.
FT   COMPBIAS   1474   1479       Poly-Ser.
FT   COMPBIAS   2148   2153       Poly-Pro.
FT   COMPBIAS   2156   2159       Poly-Pro.
FT   COMPBIAS   2341   2344       Poly-Pro.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    237    237       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    564    564       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1170   1170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1387   1387       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1622   1622       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1727   1727       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1847   1847       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1975   1975       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1985   1985       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2093   2093       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2113   2113       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2161   2161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2276   2276       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2451   2451       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2647   2647       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2654   2654       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2663   2663       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2794   2794       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2810   2810       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2865   2865       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2929   2929       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2964   2964       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3028   3028       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    940   1095       {ECO:0000250}.
FT   DISULFID   1116   1254       {ECO:0000250}.
FT   DISULFID   2971   3040       {ECO:0000250}.
FT   DISULFID   2991   3054       {ECO:0000250}.
FT   DISULFID   3004   3070       {ECO:0000250}.
FT   DISULFID   3020   3072       {ECO:0000250}.
FT   DISULFID      ?   3075       {ECO:0000250}.
FT   VARIANT    1288   1288       R -> G.
FT   VARIANT    1305   1305       T -> S.
SQ   SEQUENCE   3133 AA;  343355 MW;  E5210D5D14A7B2B2 CRC64;
     MRGGRDPVPV PVLGDYAMVC AKNGIILQWR YNVKECELSC TGGQQYTVCA DSCLRKCSDT
     ALAASGQCKP VCVEGCACSP SQLLDDNGVC VPVAKCPCIH KGLQFNAGYK EIRPGRRERE
     LCTCVGARWD CKPATPEEIQ NYPPAEDLRS NSTAQNMEFT TCETSEPLTC KNMHLPPSTQ
     TAECRPGCQC KKGQVLDTAS KRCVPATQCP CHHAGRSYPD GHLMQEECNK CECKNGNWSC
     TQRKCAGVCG AWGDSHVNTF DGTQYDFEGV CTYLLAKGAM DGTDGFDVEI QNVPCGTTGA
     TCSKSVTLKV GGAGNEEIVS LTKNAPIPDI SKLKRIKMRK AGAYVFLDVP SLGMSLQWDR
     GLRVYVKIDT MWQGRVKGLC GNYNGDMRDD FQTPSGGGMS ESSALIFADS WKLKPTCPKP
     QPVIDHCKQR PERKEWAQSV CGALKRYPFS LCAGEVGAGA YVARCERDAC DAGADCECAC
     AALAAYAHAC AHRGVTFNWR TNDLCPMQCD EVCSNYDSCV SACPVETCDN ILYYAETTAR
     CEQDTCVEGC KPKKSCPEGS VYKNDSTTEC VPRAKCKPVC MTLDGGREVL EGEIIEEDAC
     HTCRCSKKHK VCTGQPCSTE APRIQATSSS AEPATERPHE PLKCVTGWTP WINRGPAEIG
     PDGQSVESEP LPKPNELQIG KPMCKPEMMK KIECRTVNDH KTPKETGLNV ECSLENGLVC
     EEPEKTCPDF EIKVYCECEE PQDTSPPVTV TSEASSEPVS TTLATTTSRC PPGEVYQACA
     YKCDRLCDHF KKTLIAKGRC ISEMCVDGCV DESVASNGCE GSSRWRDERT CVPVKDCTCY
     NDGQIVKPGG VTESGCIKCQ CLDNSLYCDS KDCVSLNIPH QGSTHLPYIV RPVSTTITST
     TTTTTTSTTT TTTTPEPTET TTETTVPLII KSTVSPPPEC SPDNYIDLVM GDEPLPDTAF
     SASSEFSEIF APHNARLNRG PTNSGAGSWN PKVNNDKQYI QVELPRREPI YGVVLQGSPI
     FDQYVTSYEI MYGDDGNTFS TVDGPDGKPK IFRGPIDNTH PVKQMISPPI EAKVVRIRPL
     TWHDEISLRL EIIGCAEPLT TETSEPSPTS ESPLQCTEPL GLIGELPLEN IQVSSNSEEK
     DYLSINGNRG WKPLYNTPGW VMFDFTGPRN ITGILTKGGN DGWVTSYKVL YTSDFETFNP
     VIDKDGKEKI FPANFDGIVS VTNEFHPPIR ARYLKVLPQK WNKNIELRIE PIGCFEPYPE
     ILRSLPEEEE GREEPQVVRK EYGMSQEREM PNCHICPGVE AKECTCSYPE YFDGENCVPR
     AECPCVESFM TYPVGSTFRG ANCDECVCKL GGTTECKPFK ECQCDDESLV PKLSPTTCDC
     TCEPCTNGTK ICKTSKLCLA LESWCDGVQD CPDDERDCTT STARTTTTEP TVVTTVAPTQ
     AATAPPTTTT PKPVVECPKV ECPPGYIISY TTGSSSSYSR AFSSDLPPPR PRYSYQRYYR
     GRSTGGYSGY AKTGYSKGGF SKGGFSKGGY GYPSIPRSNQ AFTLDKPALT NKQPTSKEEC
     AQFKCISKLP AFKPGVVPPP VACSVVTCPA GYTLKLDKVP TGYNKCPQYE CVPPLERPVF
     CNMTGRTFNT FDGMEYKYDV CFHMLARDNK FDAWLIIVRK NCRLDGCTNE LIVMQDDQLI
     QVKPNMMVTY NNYEYTIEQT KKICFQKNSF DVDRLGNGIS ITSRKYNFTV LFNKEGDVKI
     GVLKKHMGGV DGLCGAYDGS LANERRLPDG RVATSIDEFG RSWAKPGVPA DACAPRVASA
     HKQRRAWDLC NVIAEEPFSQ CGKVLNLDKW RHICLEKICE CTDLVVNGTK RTEEQCRCLV
     LQQMAAECLA ADAGVDLASW RLMMDCPADC PPPLVHYDCY RKRCEETCAP YPNAARACPA
     QEGQCSPGCY CPDGKLRKGD QCVLPADCLD CTCTGVGTPA KYTTFEGDDL PFLGNCTYLA
     SRDRNQTGEH KYQVYATNGP CDDNANIVCT KIVHLIYEKN VIHISKDPTT KKLRTVIGKT
     AVFKYPVKEN WGTISLLNGQ DVSVTLPDIH VELTVSQLNL EFAVRVPTFL YGNRTEGLCG
     VCAGYQDFLV TSNGTVTDDF DLYGKSWQAS PEKLTELEVP SDEQCDAPPP PAPCTPPPPD
     NNTCYHLYNA DRFGACHALV EPQPYVESCE ADECGGHGPC DALQRYAAAC AELGLCLPDW
     RRELCPYPCE EPFVYRACVD CERTCDNYEQ LQTSPEKCTN KPVEGCFCPE GKVRVNNTCI
     EPGKCFPCGV DGHYAGDEWQ EDASTLCACA RSPHGTALVG CRATSCAPPV CAHGEDLRTA
     PPPPGQCCPE YDCVAKPEAQ CKETKKIVCD YGQVLKQKTN PSGCKEYFCE CKPSSECEVI
     PPESEVEIVE AGIHREIDNS GCCPRVSLVC RPETCPKPPH CPQFQTLASV NITGKCCPEY
     KCELPKDKCI VTLEWEAAAK GGEKPREKPQ TVLKDLEAVW LDGPCRSCEC ALSGAGPAAT
     CAVSACPAVV SSELFVLEPR PVPFACCPEP VQVACRHQDN VYKVGEKWKS PTDVCETYEC
     AADGDGKLQR LAAVQRCDRH CQPGWKYVPA EADSGQCCGK CEPVACVVDG EEKPIGEKWT
     SSDFCTNFTC VNLNGTLQVQ SSNETCPEIS DAERKQFVLK EQKVPGKCCP KIEREACTSG
     RSDIPGRREL DVDRELVREL PMRAGRGRRP ALRGLRAALR DRLPTRLEVL PAPAECCGRC
     KPSPASWKGG RGPSGRARER PVGESWTSAD FCTNYTCADL HGTLQVQSSN ETCPEVSEAV
     KKQFVLKEEK IPGKCCPKVE PVACRDGDKI YQEVQVWTTP DPCTNRTCRR EDGQLSVGRT
     VEHCERQCRR GWTYSPPAAD HCCGRCVQSA CLVDDQLKEP GSTWSSADNC TTFSCDRSGE
     EVFVTSATEH CPDVSACDPA DIVNTTCCQI CNEKPQALSK CVLRASELRH CRSDPHPMGA
     HGLCVNKFPI TGFTEVHGSC DSGTIYNNQT GTHESACECC QAAKYSGVSV RLTCEDGTVR
     PHRVATPARC HCAACGPGLT KHPKPGHASY TGTKNPVQPE RDREYVIPDI SSASGEARRN
     HDSNYITTLI ISF
//
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