ZAN_PIG
ID ZAN_PIG Reviewed; 2476 AA.
AC Q28983;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Zonadhesin;
DE Flags: Precursor;
GN Name=ZAN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 823-830; 859-872;
RP 883-890; 920-925; 960-967; 1235-1244; 1349-1354; 1518-1532; 1624-1656;
RP 1658-1667; 1777-1795 AND 1914-1921.
RC STRAIN=Meishan; TISSUE=Testis;
RX PubMed=7592795; DOI=10.1074/jbc.270.44.26025;
RA Hardy D.M., Garbers D.L.;
RT "A sperm membrane protein that binds in a species-specific manner to the
RT egg extracellular matrix is homologous to von Willebrand factor.";
RL J. Biol. Chem. 270:26025-26028(1995).
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.
CC -!- SUBUNIT: Probably forms covalent oligomers.
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 -!- TISSUE SPECIFICITY: In testis, primarily in haploid spermatids. Not in
CC lung, liver, heart, spleen, brain, kidney, epididymis.
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).
CC -!- PTM: The MAM domains and the mucin-like domains are missing from the
CC zonadhesin that binds to the egg extracellular matrix. Processing might
CC occur during sperm maturation and/or capacitation.
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DR EMBL; U40024; AAC48486.1; -; mRNA.
DR PIR; T34022; T34022.
DR RefSeq; NP_999548.1; NM_214383.1.
DR AlphaFoldDB; Q28983; -.
DR SMR; Q28983; -.
DR STRING; 9823.ENSSSCP00000008195; -.
DR PaxDb; Q28983; -.
DR PeptideAtlas; Q28983; -.
DR GeneID; 397676; -.
DR KEGG; ssc:397676; -.
DR CTD; 7455; -.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q28983; -.
DR OrthoDB; 22053at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:MGI.
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; PF00008; EGF; 1.
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; 4.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00214; VWC; 2.
DR SMART; SM00215; VWC_out; 3.
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; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 2.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..2476
FT /note="Zonadhesin"
FT /id="PRO_0000007785"
FT TOPO_DOM 30..2418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2419..2439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2440..2476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..144
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 147..312
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 690..739
FT /note="TIL 1"
FT DOMAIN 740..794
FT /note="VWFC 1"
FT DOMAIN 799..976
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1070..1123
FT /note="TIL 2"
FT DOMAIN 1124..1180
FT /note="VWFC 2"
FT DOMAIN 1184..1364
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1456..1511
FT /note="TIL 3"
FT DOMAIN 1512..1568
FT /note="VWFC 3"
FT DOMAIN 1573..1751
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1851..1907
FT /note="TIL 4"
FT DOMAIN 1908..1963
FT /note="VWFC 4"
FT DOMAIN 1968..2145
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2257..2310
FT /note="TIL 5"
FT DOMAIN 2311..2365
FT /note="VWFC 5"
FT DOMAIN 2366..2402
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..687
FT /note="53 X approximate heptapeptide repeats (mucin-like
FT domain)"
FT REGION 358..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1747..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2438..2476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2452
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 801..936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 823..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1186..1324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1208..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1575..1712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1597..1750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1970..2107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2370..2381
FT /evidence="ECO:0000250"
FT DISULFID 2375..2390
FT /evidence="ECO:0000250"
FT DISULFID 2392..2401
FT /evidence="ECO:0000250"
FT CONFLICT 823
FT /note="C -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="S -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="W -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="S -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2476 AA; 270365 MW; A13B690375A6548C CRC64;
MLGLPALAGP MAMPHPPLIP STPTLLAFSF PGGFYMLLDP KNAKPRQRSA LLSPLIQSSG
CLSLSFQYTQ RGQASGATLM VYASVLGSIR KHTLFSGQPG PSWQPVSVNY TSQGQIQFTL
VGVFGKIPEP AVAVDAISIA PCEESFPQCD FEDNAHPFCD WVQASQDGGY WRQGNKNTFI
QPAGPFGISL NGEGHYIFLE TDKFSQAGQS FRLVSRPFCA PAVICVTFTY HMYGLGQGTK
LRLLLGSPAG SPPSSLWERV GPQSPEWLNT SVTIPSGHQQ PMQLIFEAVR GTNTAFVVAL
GFVLINHGTC RGPSETSVST EKPVAPTEKP TVPSEIYTIP TEKPMVHMEK PIVHTEKPTV
PTEKPTIPTE KSTVPTKKPT VFKEPTLPPE GPTVPAERPT TPPEGPAVPP KGPTVLTEWP
TSHTEKSTVH TEKPILPTGK STIPTEKPMV PTKRTTTPTE RTTIPAEKPT VPIEKPMVPT
ERTTIPTERT TIPTEKPTVP TEKLTVPTEK PIVPTEKPIV PTEKHTIPTE KLTVLTERTT
TPTERTTIPT EKPTVPTEKP SVPTEKPTVP TEEPTIPTEK LTVPTERTTT PTKRTTTPTI
RTTTPTIRTT TPTERTTTPT IRTTTPTERT TIPTKKTTVP TEKTIIPTER TIAPTTPQPS
PTLVPTQPAA VVMPSTSATT VTPRTTIASC PPNAHFERCA CPVSCQSPTP NCELFCKPGC
VCDPGFLFSG SHCVNASSCD CFYNDNYYKL GTDWFSPNCT EHCHCRPSSR MECQTFKCGT
HTVCQLKNGQ YGCHPYGSAT CSVYGDPHYL TFDGRRFNFM GKCTYILAQP CGNLTEHFFR
VLVKKEERGQ EGVSCLSKVY VTLPESTVTL LKGRHTLVGG QRVTLPAIPS RGVFLAPSGR
FVELQTAFGL RVRWDGDQQL FVSVPSTFSG KLCGLCGDYD GDSSNDNQKP DGSPAKDEKE
LGSSWQTSED ADQQCEENQV SPPSCNTALQ NTMSGPEFCG QLVAPHGVFE ACLPHLRASS
FFKSCTFDMC NFQGLQHMLC AHMSALTENC QDAGYTVKPW RGPQFCPLAC PRNSRYTLCA
RLCPDTCHSE FSGRACKDRC VEGCECDPGF VLSGLQCVSR SECGCLDSTA GYVKVGERWF
KPGCRQLCIC EGNNRTRCVL WRCQAQEFCG QQDGIYGCHA QGSATCTVSG DPHYLTFDGA
LHHFTGTCTY TLTKPCWLRS LENSFLVSAT NEFRGGNLEA SYVRAVQVQV FNLRISLIKG
RKVTLDGRRV ALPLWPAQGR VSITSSGSFI LLYTDFGLQV RYDGDHLVEV TVPSSYAGRL
CGLCGNYNNN SLDDILQPDK RPASSSVRLG ASWKINELSE PGCFAEGGKP PRCLGKEVAD
AWRKNCDVLM NPQGPFSQCH RVVAPQSSFS SCLYGQCATK GDTLTLCRSL QAYASLCARA
GQALTWRNGT FCPLKCPSGS SYSTCANPCP ATCLSLNNPS YCPSTLPCAE GCECQKGHIL
SGTSCVPLSQ CGCTTQRGSY HPVGESWYTD NSCSRLCTCS AHNNISCRQA SCKPSQMCWP
QDGLIRCRVA GMGVCRIPDT SHYVSFDGSY HAVRGNCTYV LVKICHSTMD LPFFKISGEN
GKREGQPPAF YLRQVYVDIF NTLVTLKQDQ VLINGTRVSL PATTQIRGVR VISRDGYTVL
TINIGVQVKF DGRGFLEVEI PKAYYGRTCG VCGNFNDEEE DELMMPSDAL ALDDVMYVDS
WRDKEIDPNC QEDDRKTEAE SQEQPSANCR PADLERAQEQ CQAAFQAPAW ANCATRVVLS
PYVRSCTHKL CEFGGLNRAF CESLQAFGAA CQAQGIKPPV WRNSSFCPLD CSAHSVYTSC
VPSCLPSCQD PEGQCTGAGA PSTCEEGCIC EPGYVLSEQQ CVARSQCGCR DARGTFLPVG
RFRLSSGCSQ MCVCTAGAIE CRPFTCPSGS QCEPNEDGKD FCQPNSSNLC SVFGDPHYRT
FDGLSYRFQG RMTYTLVKTL DVLPDGVEPL VVEGRNKVYP SLTPVFLQEI IVMVYGYTVQ
LQAELELVVN GQKVSIPYKP NEYLQVTLRG RRLYLVTDFE LVVSFNGRNN AVIAMPSTYL
GLVRGLCGNY DKNKRNDFML PNGSFTQNLL VFGNSWEVKA KEGHPRFSRA IREEEEKNEE
SGFQNVSECS PEQLELVNHT QACGVLVDPQ GPFAACHQIV APGPFQEHCV FDLCAAPGPK
EQEELRCQVL SGYAIICQES GPTLAGWRDH THCALPCPAN TVYQSCMTPC PASCATLAVP
RACDGPCVEG CASLPGYIYS GAQSLPMAHC GCTNNGVYYQ QGDSFVTENC SQRCTCASSG
VLLCEPLSCR PGEICTLGNL TRGCFRDSPC LQNPCQNDGR CREQGTHFTC ECELGYGGDL
CTEPRGVPSP KKPEASNRVA ILLGMLMPTV LLVPAVTRVS RKRRRRRRPS RERTQSQNRG
KRAGTDCAPE QAYKVA
