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ZAN_HUMAN
ID   ZAN_HUMAN               Reviewed;        2812 AA.
AC   Q9Y493; A0A087WU49; A0FKC8; D6W5W4; O00218; Q96L85; Q96L86; Q96L87; Q96L88;
AC   Q96L89; Q96L90; Q9BXN9; Q9BZ83; Q9BZ84; Q9BZ85; Q9BZ86; Q9BZ87; Q9BZ88;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 5.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Zonadhesin;
DE   Flags: Precursor;
GN   Name=ZAN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RC   TISSUE=Testis;
RA   Cheung T.L., Wassler M.J., Cornwall G.A., Hardy D.M.;
RT   "Multiple intra-species variants of human zonadhesin.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-430; LEU-1969; THR-2035
RP   AND PRO-2111.
RX   PubMed=17033959; DOI=10.1086/508473;
RA   Gasper J., Swanson W.J.;
RT   "Molecular population genetics of the gene encoding the human fertilization
RT   protein zonadhesin reveals rapid adaptive evolution.";
RL   Am. J. Hum. Genet. 79:820-830(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-430; LEU-1969;
RP   MET-1995; THR-2035 AND PRO-2111.
RX   PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA   Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA   Tsui L.-C., Rosenthal A.;
RT   "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT   of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT   genes.";
RL   Genome Res. 8:1060-1073(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1810-2812 (ISOFORM 1), AND VARIANTS
RP   LEU-1969; THR-2035 AND PRO-2111.
RX   PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA   Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2683 (ISOFORM 7).
RC   TISSUE=Testis;
RX   PubMed=9126492; DOI=10.1006/geno.1997.4620;
RA   Gao Z., Harumi T., Garbers D.L.;
RT   "Chromosome localization of the mouse zonadhesin gene and the human
RT   zonadhesin gene (ZAN).";
RL   Genomics 41:119-122(1997).
RN   [8]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=3;
CC         IsoId=Q9Y493-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q9Y493-2; Sequence=VSP_001430, VSP_001431;
CC       Name=2;
CC         IsoId=Q9Y493-3; Sequence=VSP_001428, VSP_001429;
CC       Name=4;
CC         IsoId=Q9Y493-4; Sequence=VSP_001424, VSP_001425;
CC       Name=5;
CC         IsoId=Q9Y493-5; Sequence=VSP_001420, VSP_001421;
CC       Name=6;
CC         IsoId=Q9Y493-6; Sequence=VSP_001422, VSP_001423;
CC       Name=7;
CC         IsoId=Q9Y493-7; Sequence=VSP_001426, VSP_001427;
CC   -!- TISSUE SPECIFICITY: In testis, primarily in haploid spermatids.
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 domain 2 may mediate covalent oligomerization.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC78790.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76487.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76489.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76491.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAW76492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF332975; AAK01431.1; -; mRNA.
DR   EMBL; AF332976; AAK01432.1; -; mRNA.
DR   EMBL; AF332977; AAK01433.1; -; mRNA.
DR   EMBL; AF332978; AAK01434.1; -; mRNA.
DR   EMBL; AF332979; AAK01435.1; -; mRNA.
DR   EMBL; AF332980; AAK01436.1; -; mRNA.
DR   EMBL; EF025894; ABJ98522.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04410.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04411.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04412.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04413.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04414.1; -; Genomic_DNA.
DR   EMBL; AY046055; AAL04415.1; -; Genomic_DNA.
DR   EMBL; AC009488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF570250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471091; EAW76487.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76488.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76489.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76490.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76491.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471091; EAW76492.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF053356; AAC78790.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF312032; AAK21011.1; -; Genomic_DNA.
DR   EMBL; U83191; AAC51208.1; -; mRNA.
DR   CCDS; CCDS47663.2; -. [Q9Y493-6]
DR   CCDS; CCDS47664.2; -. [Q9Y493-1]
DR   RefSeq; NP_003377.2; NM_003386.2. [Q9Y493-1]
DR   RefSeq; NP_775082.2; NM_173059.2. [Q9Y493-6]
DR   SMR; Q9Y493; -.
DR   BioGRID; 113294; 1.
DR   STRING; 9606.ENSP00000480750; -.
DR   GlyGen; Q9Y493; 11 sites.
DR   iPTMnet; Q9Y493; -.
DR   PhosphoSitePlus; Q9Y493; -.
DR   BioMuta; ZAN; -.
DR   EPD; Q9Y493; -.
DR   jPOST; Q9Y493; -.
DR   PeptideAtlas; Q9Y493; -.
DR   PRIDE; Q9Y493; -.
DR   ProteomicsDB; 86132; -. [Q9Y493-1]
DR   ProteomicsDB; 86133; -. [Q9Y493-2]
DR   ProteomicsDB; 86134; -. [Q9Y493-3]
DR   ProteomicsDB; 86135; -. [Q9Y493-4]
DR   ProteomicsDB; 86136; -. [Q9Y493-5]
DR   ProteomicsDB; 86137; -. [Q9Y493-6]
DR   ProteomicsDB; 86138; -. [Q9Y493-7]
DR   Antibodypedia; 73512; 44 antibodies from 8 providers.
DR   DNASU; 7455; -.
DR   Ensembl; ENST00000538115.5; ENSP00000445091.2; ENSG00000146839.19. [Q9Y493-4]
DR   Ensembl; ENST00000542585.5; ENSP00000444427.2; ENSG00000146839.19. [Q9Y493-3]
DR   Ensembl; ENST00000546213.5; ENSP00000441117.2; ENSG00000146839.19. [Q9Y493-5]
DR   Ensembl; ENST00000546292.2; ENSP00000445943.2; ENSG00000146839.19. [Q9Y493-6]
DR   Ensembl; ENST00000613979.5; ENSP00000480750.1; ENSG00000146839.19. [Q9Y493-1]
DR   Ensembl; ENST00000618565.4; ENSP00000478371.1; ENSG00000146839.19. [Q9Y493-1]
DR   Ensembl; ENST00000620596.4; ENSP00000481742.1; ENSG00000146839.19. [Q9Y493-6]
DR   GeneID; 7455; -.
DR   KEGG; hsa:7455; -.
DR   MANE-Select; ENST00000613979.5; ENSP00000480750.1; NM_003386.3; NP_003377.2.
DR   UCSC; uc032zzh.1; human.
DR   CTD; 7455; -.
DR   DisGeNET; 7455; -.
DR   GeneCards; ZAN; -.
DR   HGNC; HGNC:12857; ZAN.
DR   HPA; ENSG00000146839; Not detected.
DR   MIM; 602372; gene.
DR   neXtProt; NX_Q9Y493; -.
DR   OpenTargets; ENSG00000146839; -.
DR   PharmGKB; PA37446; -.
DR   VEuPathDB; HostDB:ENSG00000146839; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   GeneTree; ENSGT00940000156850; -.
DR   InParanoid; Q9Y493; -.
DR   OMA; NHTRGCF; -.
DR   OrthoDB; 22053at2759; -.
DR   PhylomeDB; Q9Y493; -.
DR   PathwayCommons; Q9Y493; -.
DR   BioGRID-ORCS; 7455; 3 hits in 193 CRISPR screens.
DR   ChiTaRS; ZAN; human.
DR   GenomeRNAi; 7455; -.
DR   Pharos; Q9Y493; Tbio.
DR   PRO; PR:Q9Y493; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9Y493; protein.
DR   Bgee; ENSG00000146839; Expressed in left testis and 2 other tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; NAS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR   CDD; cd06263; MAM; 3.
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; 3.
DR   Pfam; PF01826; TIL; 4.
DR   Pfam; PF12714; TILa; 5.
DR   Pfam; PF00094; VWD; 4.
DR   SMART; SM00832; C8; 4.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00137; MAM; 3.
DR   SMART; SM00214; VWC; 4.
DR   SMART; SM00215; VWC_out; 4.
DR   SMART; SM00216; VWD; 4.
DR   SUPFAM; SSF49899; SSF49899; 3.
DR   SUPFAM; SSF57567; SSF57567; 4.
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; 3.
DR   PROSITE; PS51233; VWFD; 4.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..2812
FT                   /note="Zonadhesin"
FT                   /id="PRO_0000007783"
FT   TOPO_DOM        18..2757
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2758..2778
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2779..2812
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          39..204
FT                   /note="MAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          209..368
FT                   /note="MAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          371..536
FT                   /note="MAM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          1044..1093
FT                   /note="TIL 1"
FT   DOMAIN          1103..1148
FT                   /note="VWFC 1"
FT   DOMAIN          1154..1331
FT                   /note="VWFD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1426..1479
FT                   /note="TIL 2"
FT   DOMAIN          1480..1535
FT                   /note="VWFC 2"
FT   DOMAIN          1540..1720
FT                   /note="VWFD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          1812..1867
FT                   /note="TIL 3"
FT   DOMAIN          1868..1924
FT                   /note="VWFC 3"
FT   DOMAIN          1929..2108
FT                   /note="VWFD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          2211..2267
FT                   /note="TIL 4"
FT   DOMAIN          2268..2329
FT                   /note="VWFC 4"
FT   DOMAIN          2329..2505
FT                   /note="VWFD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DOMAIN          2652..2797
FT                   /note="VWFC 5"
FT   DOMAIN          2708..2744
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          61..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          573..1041
FT                   /note="66 X heptapeptide repeats (approximate) (mucin-like
FT                   domain)"
FT   REGION          904..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1302..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1685
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1804
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1900
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1946
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1156..1291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1178..1330
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1542..1680
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1564..1719
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1931..2069
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1953..2107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        2331..2468
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        2712..2723
FT                   /evidence="ECO:0000250"
FT   DISULFID        2717..2732
FT                   /evidence="ECO:0000250"
FT   DISULFID        2734..2743
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         2597..2724
FT                   /note="HGVSSRYHISELYDTLPSILCQPGRPRGLRGPLRGRLRQHPRLCLQWHPEPP
FT                   LADCGCTSNGIYYQLGSSFLTEDCSQRCTCASSRILLCEPFSCRAGEVCTLGNHTQGCF
FT                   PESPCLQNPCQNDGQCR -> YAILCQEAGAALAGWRDRTLCAMECPAGTIYQSCMTPC
FT                   PASCANLADPGDCEGPCVEGCASIPGYAYSGTQSLPWLTVAAPAMASTTRSELAAGGPG
FT                   EQRRQGEPDQGWNWNVSSWPFPFLAGQQLSD (in isoform 1)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001430"
FT   VAR_SEQ         2597..2689
FT                   /note="HGVSSRYHISELYDTLPSILCQPGRPRGLRGPLRGRLRQHPRLCLQWHPEPP
FT                   LADCGCTSNGIYYQLGSSFLTEDCSQRCTCASSRILLCEPF -> YAILCQEAGAALAG
FT                   WRDRTLCAMECPAGTIYQSCMTPCPASCANLADPGDCEGPCVEGCASIPGYAYSGTQSL
FT                   PWLTVAAPAMASTTSWAAAF (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001428"
FT   VAR_SEQ         2597..2636
FT                   /note="HGVSSRYHISELYDTLPSILCQPGRPRGLRGPLRGRLRQH -> YAILCQEA
FT                   GAALAGWRDRTLCAMECPAGTIYQSCMTPCPASCANLADPGDCEGPCVEGCAD (in
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:9126492"
FT                   /id="VSP_001426"
FT   VAR_SEQ         2597..2624
FT                   /note="HGVSSRYHISELYDTLPSILCQPGRPRG -> YAILCQEAGAALAGWRDRTL
FT                   CAGQQLSD (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001424"
FT   VAR_SEQ         2597..2617
FT                   /note="HGVSSRYHISELYDTLPSILC -> YAILCQEAGAALAGWRDRTLC (in
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001422"
FT   VAR_SEQ         2597..2601
FT                   /note="HGVSS -> WAAAF (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001420"
FT   VAR_SEQ         2602..2812
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001421"
FT   VAR_SEQ         2618..2708
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001423"
FT   VAR_SEQ         2625..2812
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001425"
FT   VAR_SEQ         2663..2666
FT                   /note="LGSS -> VRAGSRRPWGAEAPRRARPGMELERLLLALPFLAGQQ (in
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:9126492"
FT                   /id="VSP_001427"
FT   VAR_SEQ         2690..2812
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001429"
FT   VAR_SEQ         2725..2812
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001431"
FT   VARIANT         16
FT                   /note="L -> F (in dbSNP:rs12673246)"
FT                   /id="VAR_064584"
FT   VARIANT         113
FT                   /note="G -> A (in dbSNP:rs34828430)"
FT                   /id="VAR_061162"
FT   VARIANT         412
FT                   /note="G -> S (in dbSNP:rs17162408)"
FT                   /id="VAR_055785"
FT   VARIANT         430
FT                   /note="Q -> H (in dbSNP:rs221833)"
FT                   /evidence="ECO:0000269|PubMed:17033959,
FT                   ECO:0000269|PubMed:9799793"
FT                   /id="VAR_064585"
FT   VARIANT         690
FT                   /note="S -> T (in dbSNP:rs13241461)"
FT                   /id="VAR_055786"
FT   VARIANT         1012
FT                   /note="L -> R (in dbSNP:rs6942733)"
FT                   /id="VAR_055787"
FT   VARIANT         1096
FT                   /note="F -> C (in dbSNP:rs221823)"
FT                   /id="VAR_055788"
FT   VARIANT         1375
FT                   /note="A -> T (in dbSNP:rs2293767)"
FT                   /id="VAR_055789"
FT   VARIANT         1674
FT                   /note="G -> C (in dbSNP:rs10953303)"
FT                   /id="VAR_055790"
FT   VARIANT         1698
FT                   /note="L -> P (in dbSNP:rs10247980)"
FT                   /id="VAR_055791"
FT   VARIANT         1742
FT                   /note="C -> R (in dbSNP:rs17147735)"
FT                   /id="VAR_055792"
FT   VARIANT         1878
FT                   /note="P -> S (in dbSNP:rs314298)"
FT                   /id="VAR_055793"
FT   VARIANT         1903
FT                   /note="C -> Y (in dbSNP:rs12673041)"
FT                   /id="VAR_055794"
FT   VARIANT         1922
FT                   /note="H -> C (requires 2 nucleotide substitutions;
FT                   dbSNP:rs314299)"
FT                   /id="VAR_064586"
FT   VARIANT         1969
FT                   /note="F -> L (in dbSNP:rs542137)"
FT                   /evidence="ECO:0000269|PubMed:11239002,
FT                   ECO:0000269|PubMed:17033959, ECO:0000269|PubMed:9799793"
FT                   /id="VAR_064587"
FT   VARIANT         1995
FT                   /note="I -> M (in dbSNP:rs541275)"
FT                   /evidence="ECO:0000269|PubMed:9799793"
FT                   /id="VAR_059278"
FT   VARIANT         2035
FT                   /note="S -> T (in dbSNP:rs539445)"
FT                   /evidence="ECO:0000269|PubMed:11239002,
FT                   ECO:0000269|PubMed:17033959, ECO:0000269|PubMed:9799793"
FT                   /id="VAR_064588"
FT   VARIANT         2073
FT                   /note="N -> S (in dbSNP:rs314300)"
FT                   /id="VAR_059279"
FT   VARIANT         2111
FT                   /note="L -> P (in dbSNP:rs531503)"
FT                   /evidence="ECO:0000269|PubMed:11239002,
FT                   ECO:0000269|PubMed:17033959, ECO:0000269|PubMed:9799793"
FT                   /id="VAR_064589"
FT   VARIANT         2334
FT                   /note="Y -> S (in dbSNP:rs60783739)"
FT                   /id="VAR_061163"
FT   VARIANT         2349
FT                   /note="L -> F (in dbSNP:rs59541653)"
FT                   /id="VAR_061164"
FT   VARIANT         2527
FT                   /note="T -> M (in dbSNP:rs3847059)"
FT                   /id="VAR_059280"
FT   VARIANT         2643
FT                   /note="W -> R (in dbSNP:rs314339)"
FT                   /id="VAR_059281"
FT   CONFLICT        1922
FT                   /note="H -> R (in Ref. 1; AAK01431/AAK01432/AAK01433/
FT                   AAK01434/AAK01435/AAK01436 and 4; EAW76487/EAW76488/
FT                   EAW76489/EAW76490/EAW76491/EAW76492)"
FT   CONFLICT        2430
FT                   /note="W -> R (in Ref. 2; AAL04410/AAL04411/AAL04412/
FT                   AAL04413/AAL04414/AAL04415/ABJ98522, 6; AAK21011 and 7;
FT                   AAC51208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2555
FT                   /note="G -> A (in Ref. 7; AAC51208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2565
FT                   /note="A -> P (in Ref. 7; AAC51208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2761
FT                   /note="G -> A (in Ref. 1; AAK01433)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2812 AA;  305630 MW;  905BF4706FCC10F2 CRC64;
     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
     IYLEADEFSQ 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 CHPAMALPFF KISAKHEKEE
     GGTEAFRLHE VYIDIYDAQV TLQKGHRVLI NSKQVTLPAI SQIPGVSVKS SSIYSIVNIK
     IGVQVKFDGN HLLEIEIPTT YYGKVCGMCG NFNDEEEDEL MMPSDEVANS DSEFVNSWKD
     KDIDPSCQSL LVDEQQIPAE 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 PNEHLRVTLW 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
 
 
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