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 27-MAR-2024, entry version 135.
DE RecName: Full=Hemocytin;
DE AltName: Full=Humoral lectin;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC 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 lectin
RT 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 encapsulation
CC 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 viral
CC infection and inhibited by D-mannose, N-acetyl-D-galactosamine and D-
CC maltose.
CC -!- PTM: May be converted into the 260 kDa mature hemocytin by proteolysis.
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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.P98092; -.
DR PaxDb; 7091-BGIBMGA006692-TA; -.
DR EnsemblMetazoa; NM_001111347.1; NP_001104817.1; LOC692743.
DR GeneID; 692743; -.
DR KEGG; bmor:692743; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_361397_0_0_1; -.
DR InParanoid; P98092; -.
DR OrthoDB; 5398470at2759; -.
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 CDD; cd19941; TIL; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR PANTHER; PTHR11339:SF373; HEMOLECTIN, ISOFORM A; 1.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF01826; TIL; 2.
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; SSF57603; FnI-like domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF57567; Serine protease inhibitors; 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; Disulfide bond; Glycoprotein; Lectin; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..3133
FT /note="Hemocytin"
FT /id="PRO_0000021445"
FT DOMAIN 40..96
FT /note="TIL 1"
FT DOMAIN 153..209
FT /note="TIL 2"
FT DOMAIN 247..418
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 509..576
FT /note="TIL 3"
FT DOMAIN 770..837
FT /note="TIL 4"
FT DOMAIN 940..1095
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1116..1254
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1619..1794
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1890..1948
FT /note="TIL 5"
FT DOMAIN 1951..2136
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2229..2285
FT /note="TIL 6"
FT DOMAIN 2553..2622
FT /note="VWFC 1"
FT DOMAIN 2842..2907
FT /note="VWFC 2"
FT DOMAIN 2971..3076
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2647
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 271..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 295..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 940..1095
FT /evidence="ECO:0000250"
FT DISULFID 1116..1254
FT /evidence="ECO:0000250"
FT DISULFID 1621..1754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1641..1793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1953..2099
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2001..2009
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2971..3040
FT /evidence="ECO:0000250"
FT DISULFID 2991..3054
FT /evidence="ECO:0000250"
FT DISULFID 3004..3070
FT /evidence="ECO:0000250"
FT DISULFID 3020..3072
FT /evidence="ECO:0000250"
FT DISULFID ?..3075
FT /evidence="ECO:0000250"
FT VARIANT 1288
FT /note="R -> G"
FT VARIANT 1305
FT /note="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
//
