ZAN_HUMAN » Zonadhesin

ZAN_HUMAN » Zonadhesin
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
ZAN_HUMAN » Zonadhesin »
Hydrophobic Thickness 33.2 ± 1.6 Å
Tilt Angle 1 ± 0°
ΔGtransfer -24.3 kcal/mol
ΔGfold -15.3 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 2759-2781 (2756-2790)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 41-203, PDBID: 4GWM, Subunit A, Seq Identity:22%, MAM domain, meprin/A5/mu

AA: 211-367, PDBID: 2C9A, Subunit A, Seq Identity:21%, MAM domain, meprin/A5/mu

AA: 373-535, PDBID: 2C9A, Subunit A, Seq Identity:18%, MAM domain, meprin/A5/mu

AA: 1044-1093, PDBID: 1CCV, Subunit A, Seq Identity:37%, Trypsin Inhibitor like cysteine rich domain

AA: 1094-1148, TILa domain

AA: 1156-1308, von Willebrand factor type D domain

AA: 1354-1422, C8 domain

AA: 1426-1479, PDBID: 1CCV, Subunit A, Seq Identity:30%, Trypsin Inhibitor like cysteine rich domain

AA: 1480-1535, TILa domain

AA: 1542-1697, von Willebrand factor type D domain

AA: 1741-1808, C8 domain

AA: 1812-1867, PDBID: 1CCV, Subunit A, Seq Identity:31%, Trypsin Inhibitor like cysteine rich domain

AA: 1868-1924, TILa domain

AA: 1931-2086, von Willebrand factor type D domain

AA: 2140-2207, C8 domain

AA: 2211-2267, PDBID: 1CCV, Subunit A, Seq Identity:29%, Trypsin Inhibitor like cysteine rich domain

AA: 2268-2324, TILa domain

AA: 2331-2485, von Willebrand factor type D domain

AA: 2546-2599, C8 domain

AA: 2653-2707, TILa domain

UniProt annotation for ZAN_HUMAN » Zonadhesin
FUNCTION: Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling.

SUBUNIT: Probably forms covalent oligomers.

TISSUE SPECIFICITY: In testis, primarily in haploid spermatids.

DOMAIN: The MAM domains probably mediate sperm adhesion to the zona pellucida.

DOMAIN: During sperm migration through the reproductive tracts, the mucin-like domain might inhibit inappropriate trapping of spermatozoa or promoting adhesion to the oviductal isthmus.

DOMAIN: The VWFD domain 2 may mediate covalent oligomerization.

UniProt features for ZAN_HUMAN » Zonadhesin
SIGNAL 1 17 Potential.
CHAIN 18 2812 Zonadhesin.
DOMAIN 39 204 MAM 1.
DOMAIN 209 368 MAM 2.
DOMAIN 371 536 MAM 3.
DOMAIN 1044 1093 TIL 1.
DOMAIN 1103 1148 VWFC 1.
DOMAIN 1155 1371 VWFD 1.
DOMAIN 1426 1479 TIL 2.
DOMAIN 1480 1535 VWFC 2.
DOMAIN 1541 1758 VWFD 2.
DOMAIN 1812 1867 TIL 3.
DOMAIN 1868 1924 VWFC 3.
DOMAIN 1930 2144 VWFD 3.
DOMAIN 2211 2267 TIL 4.
DOMAIN 2268 2329 VWFC 4.
DOMAIN 2330 2537 VWFD 4.
DOMAIN 2652 2797 VWFC 5.
DOMAIN 2708 2744 EGF-like.
REGION 573 1041 66 X heptapeptide repeats (approximate) (mucin-like domain).
DISULFID 2712 2723 By similarity.
DISULFID 2717 2732 By similarity.
DISULFID 2734 2743 By similarity.
Amino Acid Sequence for ZAN_HUMAN » Zonadhesin
MVPPVWTLLL LVGAALFRKE KPPDQKLVVR SSRDNYVLTQ CDFEDDAKPL CDWSQVSADD EDWVRASGPS PTGSTGAPGG YPNGEGSYLH MESNSFHRGG VARLLSPDLW EQGPLCVHFA HHMFGLSWGA QLRLLLLSGE EGRRPDVLWK HWNTQRPSWM LTTVTVPAGF TLPTRLMFEG TRGSTAYLDI ALDALSIRRG SCNRVCMMQT CSFDIPNDLC DWTWIPTASG AKWTQKKGSS GKPGVGPDGD FSSPGSGCYM LLDPKNARPG QKAVLLSPVS LSSGCLSFSF HYILRGQSPG AALHIYASVL GSIRKHTLFS GQPGPNWQAV SVNYTAVGRI QFAVVGVFGK TPEPAVAVDA TSIAPCGEGF PQCDFEDNAH PFCDWVQTSG DGGHWALGHK NGPVHGMGPA GGFPNAGGHY IYLEADEFSH AGQSVRLVSR PFCAPGDICV EFAYHMYGLG EGTMLELLLG SPAGSPPIPL WKRVGSQRPY WQNTSVTVPS GHQQPMQLIF KGIQGSNTAS VVAMGFILIN PGTCPVKVLP ELPPVSPVSS TGPSETTGLT ENPTISTKKP TVSIEKPSVT TEKPTVPKEK PTIPTEKPTI STEKPTIPSE KPNMPSEKPT IPSEKPTILT EKPTIPSEKP TIPSEKPTIS TEKPTVPTEE PTTPTEETTT SMEEPVIPTE KPSIPTEKPS IPTEKPTISM EETIISTEKP TISPEKPTIP TEKPTIPTEK STISPEKPTT PTEKPTIPTE KPTISPEKPT TPTEKPTISP EKLTIPTEKP TIPTEKPTIP TEKPTISTEE PTTPTEETTI STEKPSIPME KPTLPTEETT TSVEETTIST EKLTIPMEKP TISTEKPTIP TEKPTISPEK LTIPTEKLTI PTEKPTIPIE ETTISTEKLT IPTEKPTISP EKPTISTEKP TIPTEKPTIP TEETTISTEK LTIPTEKPTI SPEKLTIPTE KPTISTEKPT IPTEKLTIPT EKPTIPTEKP TIPTEKLTAL RPPHPSPTAT GLAALVMSPH APSTPMTSVI LGTTTTSRSS TERCPPNARY ESCACPASCK SPRPSCGPLC REGCVCNPGF LFSDNHCIQA SSCNCFYNND YYEPGAEWFS PNCTEHCRCW PGSRVECQIS QCGTHTVCQL KNGQYGCHPY AGTATCLVYG DPHYVTFDGR HFGFMGKCTY ILAQPCGNST DPFFRVTAKN EEQGQEGVSC LSKVYVTLPE STVTLLKGRR TLVGGQQVTL PAIPSKGVFL GASGRFVELQ TEFGLRVRWD GDQQLYVTVS STYSGKLCGL CGNYDGNSDN DHLKLDGSPA GDKEELGNSW QTDQDEDQEC QKYQVVNSPS CDSSLQSSMS GPGFCGRLVD THGPFETCLL HVKAASFFDS CMLDMCGFQG LQHLLCTHMS TMTTTCQDAG HAVKPWREPH FCPMACPPNS KYSLCAKPCP DTCHSGFSGM FCSDRCVEAC ECNPGFVLSG LECIPRSQCG CLHPAGSYFK VGERWYKPGC KELCVCESNN RIRCQPWRCR AQEFCGQQDG IYGCHAQGAA TCTASGDPHY LTFDGALHHF MGTCTYVLTR PCWSRSQDSY FVVSATNENR GGILEVSYIK AVHVTVFDLS ISLLRGCKVM LNGHRVALPV WLAQGRVTIR LSSNLVLLYT NFGLQVRYDG SHLVEVTVPS SYGGQLCGLC GNYNNNSLDD NLRPDRKLAG DSMQLGAAWK LPESSEPGCF LVGGKPSSCQ ENSMADAWNK NCAILINPQG PFSQCHQVVP PQSSFASCVH GQCGTKGDTT ALCRSLQAYA SLCAQAGQAP AWRNRTFCPM RCPPGSSYSP CSSPCPDTCS SINNPRDCPK ALPCAESCEC QKGHILSGTS CVPLGQCGCT DPAGSYHPVG ERWYTENTCT RLCTCSVHNN ITCFQSTCKP NQICWALDGL LHCRASGVGV CQLPGESHYV SFDGSNHSIP DACTLVLVKV CHPAMALPLF KISAKHEKEE GGTEAFRLHE VYIDIYDAQV TLQKGHRVLI NSKQVTLPAI SQIPGVSVKS SSIYTIVNIK IGVQVKFDGN HLLEIEIPTT YYGKVCGMCG NFNDEEEDEL MMPSDEVANS DSEFVNSWKD KDIDPSCQSL PVDEQQIPAE QQENPSGNCR AADLRRAREK CEAALRAPVW AQCASRIDLT PFLVDCANTL CEFGGLYQAL CQALQAFGAT CQSQGLKPPL WRNSSFCPLE CPAYSSYTNC LPSCSPSCWD LDGRCEGAKV PSACAEGCIC QPGYVLSEDK CVPRSQCGCK DAHGGSIPLG KSWVSSGCTE KCVCTGGAIQ CGDFRCPSGS HCQLTSDNSN SNCVSDKSEQ CSVYGDPRYL TFDGFSYRLQ GRMTYVLIKT VDVLPEGVEP LLVEGRNKMD PPRSSIFLQE VITTVYGYKV QLQAGLELVV NNQKMAVPYR PNEHLRVTLR GQRLYLVTDF ELVVSFGGRK NAVISLPSMY EGLVSGLCGN YDKNRKNDMM LPSGALTQNL NTFGNSWEVK TEDALLRFPR AIPAEEEGQG AELGLRTGLQ VSECSPEQLA SNSTQACRVL ADPQGPFAAC HQTVAPEPFQ EHCVLDLCSA QDPREQEELR CQVLSGHGVS SRYHISELYD TLPSILCQPG RPRGLRGPLR GRLRQHPRLC LQWHPEPPLA DCGCTSNGIY YQLGSSFLTE DCSQRCTCAS SRILLCEPFS CRAGEVCTLG NHTQGCFPES PCLQNPCQND GQCREQGATF TCECEVGYGG GLCMEPRDAP PPRKPASNLV GVLLGLLVPV VVVLLAVTRE CIYRTRRKRE KTQEGDRLAR LVDTDTVLDC AC