ZAN_RABIT
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 25-MAY-2022, entry version 113.
DE RecName: Full=Zonadhesin;
DE Flags: Fragment;
GN Name=ZAN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; 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 binding.";
RL Biol. Reprod. 65:1691-1700(2001).
CC -!- FUNCTION: Binds in a species-specific manner to the zona pellucida of
CC the egg. May be involved in gamete recognition and/or signaling (By
CC 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 zona
CC pellucida.
CC -!- DOMAIN: During sperm migration through the reproductive tracts, the
CC mucin-like domain might inhibit inappropriate trapping of spermatozoa
CC or promoting adhesion to the oviductal isthmus.
CC -!- DOMAIN: The VWFD domains 2 and 3 may mediate covalent oligomerization
CC (By similarity to human intestinal mucin MUC2).
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DR EMBL; AF244982; AAF63342.2; -; mRNA.
DR RefSeq; NP_001075550.1; NM_001082081.1.
DR AlphaFoldDB; 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 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; 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; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..2282
FT /note="Zonadhesin"
FT /id="PRO_0000055637"
FT TOPO_DOM <1..2235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2236..2256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2257..2282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..147
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 150..315
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 501..550
FT /note="TIL 1"
FT DOMAIN 551..605
FT /note="VWFC 1"
FT DOMAIN 610..787
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 881..934
FT /note="TIL 2"
FT DOMAIN 935..990
FT /note="VWFC 2"
FT DOMAIN 995..1176
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1267..1322
FT /note="TIL 3"
FT DOMAIN 1323..1379
FT /note="VWFC 3"
FT DOMAIN 1384..1564
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1670..1726
FT /note="TIL 4"
FT DOMAIN 1727..1782
FT /note="VWFC 4"
FT DOMAIN 1787..1963
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2076..2129
FT /note="TIL 5"
FT DOMAIN 2130..2184
FT /note="VWFC 5"
FT DOMAIN 2185..2221
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 315..498
FT /note="26 X approximate heptapeptide repeats (mucin-like
FT domain)"
FT REGION 333..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 612..747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 634..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 997..1136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1019..1175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1386..1525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1408..1563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1789..1926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2189..2200
FT /evidence="ECO:0000250"
FT DISULFID 2194..2209
FT /evidence="ECO:0000250"
FT DISULFID 2211..2220
FT /evidence="ECO:0000250"
FT NON_TER 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
