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Database: UniProt
Entry: P57999
LinkDB: P57999
Original site: P57999 
ID   ZAN_RABIT               Reviewed;        2282 AA.
AC   P57999;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   16-JAN-2019, entry version 105.
DE   RecName: Full=Zonadhesin;
DE   Flags: Fragment;
GN   Name=ZAN;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=11717130; DOI=10.1095/biolreprod65.6.1691;
RA   Lea I.A., Sivashanmugam P., O'Rand M.G.;
RT   "Zonadhesin: characterization, localization, and zona pellucida
RT   binding.";
RL   Biol. Reprod. 65:1691-1700(2001).
CC   -!- FUNCTION: Binds in a species-specific manner to the zona pellucida
CC       of the egg. May be involved in gamete recognition and/or signaling
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Probably forms covalent oligomers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Exclusively on the apical region of the sperm head.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The MAM domains probably mediate sperm adhesion to the
CC       zona pellucida.
CC   -!- DOMAIN: During sperm migration through the reproductive tracts,
CC       the mucin-like domain might inhibit inappropriate trapping of
CC       spermatozoa or promoting adhesion to the oviductal isthmus.
CC   -!- DOMAIN: The VWFD domains 2 and 3 may mediate covalent
CC       oligomerization (By similarity to human intestinal mucin MUC2).
DR   EMBL; AF244982; AAF63342.2; -; mRNA.
DR   RefSeq; NP_001075550.1; NM_001082081.1.
DR   UniGene; Ocu.2652; -.
DR   ProteinModelPortal; P57999; -.
DR   SMR; P57999; -.
DR   STRING; 9986.ENSOCUP00000025091; -.
DR   PRIDE; P57999; -.
DR   GeneID; 100008761; -.
DR   KEGG; ocu:100008761; -.
DR   CTD; 7455; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   eggNOG; ENOG41121S4; LUCA.
DR   HOGENOM; HOG000168448; -.
DR   HOVERGEN; HBG000375; -.
DR   InParanoid; P57999; -.
DR   OrthoDB; 22053at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd06263; MAM; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
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; Unchr_dom_Cys-rich.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF08742; C8; 4.
DR   Pfam; PF00629; MAM; 2.
DR   Pfam; PF01826; TIL; 5.
DR   Pfam; PF12714; TILa; 5.
DR   Pfam; PF00094; VWD; 4.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00214; VWC; 4.
DR   SMART; SM00215; VWC_out; 4.
DR   SMART; SM00216; VWD; 4.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   SUPFAM; SSF57567; SSF57567; 5.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50060; MAM_2; 2.
DR   PROSITE; PS51233; VWFD; 4.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN        <1   2282       Zonadhesin.
FT                                /FTId=PRO_0000055637.
FT   TOPO_DOM     <1   2235       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2236   2256       Helical. {ECO:0000255}.
FT   TOPO_DOM   2257   2282       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       <1    147       MAM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      150    315       MAM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      501    550       TIL 1.
FT   DOMAIN      551    605       VWFC 1.
FT   DOMAIN      611    826       VWFD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN      881    934       TIL 2.
FT   DOMAIN      935    990       VWFC 2.
FT   DOMAIN      996   1213       VWFD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     1267   1322       TIL 3.
FT   DOMAIN     1323   1379       VWFC 3.
FT   DOMAIN     1385   1591       VWFD 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     1670   1726       TIL 4.
FT   DOMAIN     1727   1782       VWFC 4.
FT   DOMAIN     1788   1991       VWFD 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     2076   2129       TIL 5.
FT   DOMAIN     2130   2184       VWFC 5.
FT   DOMAIN     2185   2221       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      315    498       26 X approximate heptapeptide repeats
FT                                (mucin-like domain).
FT   CARBOHYD    112    112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    272    272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    569    569       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1141   1141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1259   1259       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1270   1270       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1355   1355       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1467   1467       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1483   1483       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1662   1662       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1997   1997       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2178   2178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   2189   2200       {ECO:0000250}.
FT   DISULFID   2194   2209       {ECO:0000250}.
FT   DISULFID   2211   2220       {ECO:0000250}.
FT   NON_TER       1      1
SQ   SEQUENCE   2282 AA;  248292 MW;  380FA81093454892 CRC64;
     MFFATGRASA FSHPCGRTAV SLREERRIKK RKRQDGFYML LDPKNAKPRQ KSVLLSPLSQ
     SAGCLTLSFH YTLWGQSPGA ALSVLASVLG SIRKHTLFSG QPSPNWQPVS VNYSGPGQIQ
     FTVVGVFGDV PEPAVAVDAI SIAPCGESFP QCVFEDAAHP FCDWLQASED GGRWAWTDKD
     MLAQERSLMR ESPHTGHHYI YLEADKFSRP GQSVRLVSRP FCAPGDVCVE FSYHMYGLGE
     GTTLQFLLGS PAGSTPVSLW NRVGSQSPDW LNASVTIPSG HQQPMQLVFE AIRGSNTAFV
     VAMSFILINH GTCHVPVPPV IPIKTLVIPT EQPTVPAEGT TEPPEGTIEL PEGTTKLPEE
     TTELPEEITE PPKETTIPTE PPTVPTEPPT VPTEPPTVPT EKPTVLTEKP TVPTEETSIP
     TEPPTVPTEK PTVATEPPTV PTEEPTVATE KPTVPTEETT PPTTARSTLT SLEPTTHTPS
     TSLTSTTLST TTTPSPTTVS CPANAHYESC ACPASCKHPK ASCKPPCQPG CVCDPGLVFS
     NNSCIKASSC PCLYNNNNYE PEAEWFSPNC TELCHCWPGG RIECQISQCK THTKCQLKNG
     QYECQPYGTA TCFVYGDPHY VTFDGRHFGF MGKCTYIVAQ PCSKSTDSFF RVTAKNEERG
     QEGMSCLSRV DVTLSETVVT LLKGRRTLVG GQRVTLPAMP AKGVFLGPSG RFVELQTDFG
     LRVRWDGDQQ LLVTVPSAYF QKLCGLCGNY DGHSSNDNLK ADGQPAQSEE ELGNSWQWAQ
     DEDKECQKNQ ANPPSCDTAL QTKMSGPQFC GQLVDSRGVF KTCLLHLKAS SFFDNCVFDT
     CNFQGLQLML CAHMSAVTAA CQDAGYAVKP WREPQFCPLA CPPNSRYSLC TSPCPKTCHT
     GYVGMPCPEQ CLEGCECNPG FILSGLECVP SAQCGCLDPS RGYFKVGEQW FKSDCKQLCI
     CEGSNQIRCQ PWKCGPHEVC SQQSGIYGCH SQGSATCSAS GDPHYLTFDG ALHHFMGTCN
     YVLTQPCRHR PQENSFVVSA TNEIRDGNLE VSLRPSCPRC RSSALKISLV KGHKVVLNGR
     RVALPVWPSR GQVTVRPSGN FMLLYTNFGL RVRYDGNHLV EVTVPSSYAG QLCGLCGNYN
     NNSLDDILGP YKRPVGNSVQ LGAAWKLEEG SETGCFLQGG KPSSCHEDMG DTWNKNCEVL
     VNPLGPFSQC HKVVPPEVSF TSCVHGQCGT KGDSLTLCRS LQAYASLCSL AGQALAWRNS
     TFCPLKCPPN SSYSPCGSPC PGTCLSLNHP KDCPITLPCV EGCECQNGYI LSGTSCVPLN
     QCGCTDFEGS YHLVRESWYT DNTCSRLCTC SLHNNITCRQ TACKPGQQCW AVDGLLRCRD
     SGMGVCQVTG DSRYLSFDGS SHPLQGACTY VLAKVCHPNM DLPFFKVSAS NEKSSAGGTN
     AVSLHQVYIE FSGSLVTLQK GNLVLINGTR VALPATSQIR GLNISSSRTH TIVSFWIGAQ
     IKFDGNHVLK ITIPAAYYEK VCGICGNYNG EPEDELMMPS DELAASDLEF VKSWKDNNID
     PNCQKSQEGK GKPQEEQGPS GSSKKASCSP ADLQKVQEQC QAALQTPAWA ECASRVDLRP
     FLLDCMNSLC EFRGSLQPLC KALQALGAAC RSKGLQPPIW RNSSFCPLAC PAYSTYTNCL
     PSCSPSCFDP DGRCEGARAP SSCAEGCTCQ PGYVLSKNKC VAKDQCSCRD AQGGSIPSGK
     SWVSSGCSQK CACTEGSIQC RAFHCPSRSH CKLNSNGNSN CVSEKSDQCS IFGGPHYRTF
     DRFSFGFRGR MTYVLIKTVD ELPDGVERLL VQARNKMYPP WNKVFLQEII TTVYGYKVQL
     QRDLVLVVNN QKMAVPYKPE DRLRVSMQGQ RLFLITDFEM VVSFDGRNAA VITLPSMYQG
     LVRGLCGNYD SDRRNEMMLP NGAITTNVDV FGNSWEVKTE DSVLRFRRAL QVEADGKEKE
     TGSYRSECSQ EQLALVNSTQ ACRVLVDPQG PFAACHQTVA PEPFQEHCVS DLCASRDPKE
     HEELRCQVLS GYSITCQEAG IALAGWRDHT HCAMVCPANT VYQSCMTPCP ESCANLAAPR
     DCEGPCVEGC ASLPGYAFSG AQSLPLANCG CTSNGIYYQL GHSFVTADCS QRCTCASSGV
     LLCEPFSCRP GESCTLGNLT RGCFRESPCL RNPCQNDGRC REQGTSFTCE CEPGYGGHLC
     TEPRDVLLPP KPDTSNLVAI LLGMLVSLVV TVPVLARKCV SRKRRRWREK TQSEPRSAPG
     RR
//
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