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Database: UniProt
Entry: W5MEX7_LEPOC
LinkDB: W5MEX7_LEPOC
Original site: W5MEX7_LEPOC 
ID   W5MEX7_LEPOC            Unreviewed;      1662 AA.
AC   W5MEX7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Zonadhesin {ECO:0008006|Google:ProtNLM};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006936.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000006936.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01015208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000006936; -.
DR   Ensembl; ENSLOCT00000006944.1; ENSLOCP00000006936.1; ENSLOCG00000005742.1.
DR   eggNOG; KOG1216; Eukaryota.
DR   GeneTree; ENSGT00940000156850; -.
DR   HOGENOM; CLU_001167_0_0_1; -.
DR   InParanoid; W5MEX7; -.
DR   OMA; PACNETD; -.
DR   Proteomes; UP000018468; Linkage group LG14.
DR   Bgee; ENSLOCG00000005742; Expressed in mesonephros and 1 other cell type or tissue.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   CDD; cd19941; TIL; 4.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR025615; TILa_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR   PANTHER; PTHR46160:SF4; VWFD DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08742; C8; 4.
DR   Pfam; PF01826; TIL; 4.
DR   Pfam; PF12714; TILa; 4.
DR   Pfam; PF00094; VWD; 4.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00214; VWC; 4.
DR   SMART; SM00215; VWC_out; 3.
DR   SMART; SM00216; VWD; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 4.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS51233; VWFD; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          118..289
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          495..669
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          818..867
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          887..1066
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          1277..1449
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
SQ   SEQUENCE   1662 AA;  185138 MW;  29193E63AEFCEF36 CRC64;
     PVCTPNSHYD SCASACPATC ALPNAPFSCE WPCVEGCVCN IGYLLNEGRC VPSNQCGCWD
     NGVYYSPGSG FWTDDTCSTQ CTCPSLGGHL TCSSASCPSD HYCGISSGVP DCYPSTFGIC
     KLHNGPHYNT FENTLHQFMG TCTYTLAKLC MKSSSIPYFS VKVKIENRGN FSNFYIHELH
     VNVYNYIISM FKELRDKVNG LWRKLPVSLS GESVRIHKRG RLIVLKTGFD LKLSYNADYM
     VEVKVPSLYF NKTCGMCGNY NHFRQNLLVK DKTEIQSSWQ DSPGDLTCEP TVPPHPCPHS
     KEQNYKGDQM CGLITSTNGY FSQCLSVVNP ESFFQQCVFH MCAQNGDLNV LCNILQAYAD
     ACQSAGLILP IWRNASFCPL TCTANSHYNS CTSACPETCM DRDAPATCKR PCVEGCECDN
     GFLLSGGRCI VPDNCGCWVN GQYYEKEDTF MDGNCESMCR CLGNNNITCS PVSCRQDEVC
     KIKDGFLGCF RTSAATCHIF GDPHYSTFDG KLYHLQGSCN YTVVQTCVNS SVHFTVSSRN
     EHRVIPGLSA LNSVALEVQG LHIALRKDKN VYINGMLATL PVLESKIHVF YEGSYIHVET
     TFGLRLLFDG DHSLFVQIDE RYKGKICGLC GTYSDSQLDD FMTPDGTLVH SPEDFGKSWR
     IQDDEWICNS DPPPVLPCNP QLDSEAFQKC SVLFAAPGPF EKCHWFIPPQ LYVDSCVYDH
     CATGGDVHQL CTSLESYAAA CEVAKVNLGN WREKTICVLT CPLNCNFDSD TRIGPVNAEM
     ICQHAHCPIR SVNFDICIVL FIKSHNLFKN GIVIVCLLDC NFEKDFCGWS QPLTGSLHWT
     RHLETTSSTF SGPSFNHTTR VYQYFTGNIC KDQLIVFPII VIVSGASFCH IAGDPHYFTF
     DKVMHTFVGA CAYTLVKVCQ TDGSVTPITI SGLNEAHGQP EATYLKQVDI TVYNNKLSIL
     KDKQLLLNGK EISNMDQPLA KGITVTSQRL YTTVLTDFGV SVKFDGKQHL EIRLPPEYFS
     KVCGMCGNNN NRQDDELLLP DGQLAHNVSH FGNSWKIDED SPPECLADER EDLGSPCKTD
     QKPEIEKQCE VLLSETFKPC HSVIPPEHFI ESCVYDMCKY LGMISTLCDM IQAYVSACRS
     EGVHINWRRG DFCPLSCPKN SHYTVCVPAC QPTCADLHAS VHCDKVQSCV EGCVCNNGYV
     LSEDKCVPIR KCGCQDKKGN YYKVSESWIT DHCSQKCKCE EEDDHAEIDC DDYGCDDDSV
     CALSENGEYK CKPTDFSECS VSGDPEYKTF DNMEHQFEGR HSYILVQTVH IPKDLPEIYI
     EGINGLKGLT TLKEIKIRVY NHTVKFKHKR KLVLDGEKVK PPTIPHRGMK ITQRSSLLFL
     ETDFGLSVKF DGHDHAEITL PYTYQNKIVG LCGNYDGDKN NDFMKPDGSQ AKNMNEFGES
     WQVQTSHSDA AIQDYNNTGV SATISFQCTE QQKTLLNSMR FCGIISDPQG PFSTCHGAVQ
     PVKHLENCVA DQCSSFNNTS LLCKSLQRYS EACQKRGISI GNWRASTLCE MKCPSHSEYR
     LCMTACPPSC GNLANPRDCE APCQEGCQCL PGFVHSNFDC VPYKECGCFY HNVYHKDGET
     FVTEDCAQNC TCSDTSVTCR PMKCPSGLVC RTSNMIRGCY EA
//
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