ID Q5DWF3_HALAU Unreviewed; 1208 AA.
AC Q5DWF3;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Vitelline coat protein VC130 {ECO:0000313|EMBL:BAD90011.1};
GN Name=vc130 {ECO:0000313|EMBL:BAD90011.1};
OS Halocynthia aurantium (Sea peach).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=254849 {ECO:0000313|EMBL:BAD90011.1};
RN [1] {ECO:0000313|EMBL:BAD90011.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16154559; DOI=10.1016/j.ydbio.2005.08.004;
RA Ban S., Harada Y., Yokosawa H., Sawada H.;
RT "Highly polymorphic vitelline-coat protein HaVC80 from the ascidian,
RT Halocynthia aurantium: structural analysis and involvement in self/nonself
RT recognition during fertilization.";
RL Dev. Biol. 286:440-451(2005).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AB188531; BAD90011.1; -; mRNA.
DR AlphaFoldDB; Q5DWF3; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 9.
DR Gene3D; 2.10.25.10; Laminin; 13.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001507; ZP_dom.
DR PANTHER; PTHR12916; CYTOCHROME C OXIDASE POLYPEPTIDE VIC-2; 1.
DR PANTHER; PTHR12916:SF4; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 13.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS51034; ZP_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1208
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004255243"
FT TRANSMEM 1167..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..65
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 78..114
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 127..171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 183..227
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 238..282
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 292..336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 344..388
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 397..441
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 450..494
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 502..546
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 555..599
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 609..653
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 663..707
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 717..754
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 818..1083
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT DISULFID 55..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 104..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 161..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 217..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 272..281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 326..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 378..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 431..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 484..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 536..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 589..598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 643..652
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 697..706
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 744..753
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1208 AA; 130234 MW; A1195040935287C3 CRC64;
MNSLKFSFLL LLCSVAEVLG VTNYCTTNPN PCINGGACVD PSTDQTVQSW YICRCLASYS
GEHCEISMVV PSDLIGVEVF NCYTNPCLNG GLCVNGIQGG YCQCPSTATG TRCETRIIID
PIQSPGTSAY CTTFGNRCVN GGSCIDRTTS PTLTSWYICS CPIGYTGDHC EVGGGSQNPD
VYYTYYCSRI GNPCQNGGLC VDRSSRPSIT SWYMCSCISG YSGDHCEIIG GQGNGGVYTD
YCRLVANPCG NGGSCTDRTT NPFIASLYTC TCLYGFSGVH CEIRDTQTDG GVNNYCTINP
NPCINGGQCV DRTQDSTIVS WYICRCHGGY SGDHCEIGGQ GNAVVNYCRL VANPCRNGGS
CTDRTTNPFI ASLYTCTCLH GFSGVHCEIS GTQIDGGVNY CTVNPNPCIN GGQCVDRTQD
STIVSWYICR CHGGYSGDHC EIRGVEIDGG VNYCTVNPNP CINGGQCVDK SQDSTVVSWY
ICRCHGGYSG DHCEIGGQDN AVMNYCRLVA NPCINGGSCT DRSTNPFIAS LYTCTCLHGF
SGVHCEIRSI PNDVGNNYCT VNPNPCINGG QCVDKSQDFT IASWYICRCH GGYSGDHCEI
GGQVNVGLYI GYCGRMTNPC RNGGSCTDRT TNPSIASGYT CRCLFGFSGD HCELRGVQID
GGADNYCTVN PNPCINGGQC VDMTQDSYII SGYICRCHGG YSGDHCENGN YIMGRAGAAI
CEDYNPCRNG GICKYDDGSF SCECPERCNG PLCDDCGEIP DPVGSGFEDY YSSYVCNPNP
CKGDCICQPS CRHSNGYICK STSGFLGKDC TIPVPKLICD TDRITITVSE GFVREYDRQL
DNSLILISPD SRVTPSSCVV KMSTNGFYTY TILFPFDTCG TTKNSTSGGE VYTNIMWFNK
VLSNTLFDVP VPAARFQCTY RREYNVITSL RPVAPTVETI YDSMTTLPSI SLCKSPACPG
TCPDHLSVSR GGFYTVGETI YVTMHLDIAD LVDRGIVNTI HNMFLSCSEN PDQTPDAIYI
VQNGCGTSSG LPCDISHTGK GATVCVNFDT PRLPNCNQFF IHAELRSCKS TSLKTCTSVQ
SSYCTTNSWD RKKRAISNDT TTAEAYTVIG PIFIVTNASE GVPRVELFPE DVPETLSAVD
FSSLGDNETD DNDTPEEPRP VKSRLQVWIL ILAAVLVVSL LSFAFVVSFV CKSKYEDGDL
LVPKSPSV
//
