ID   SEMG1_HUMAN             Reviewed;         462 AA.
AC   P04279; Q53ZV0; Q53ZV1; Q53ZV2; Q6X4I9; Q6Y809; Q6Y822; Q6Y823; Q86U64;
AC   Q96QM3;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   27-MAR-2024, entry version 219.
DE   RecName: Full=Semenogelin-1;
DE   AltName: Full=Cancer/testis antigen 103;
DE   AltName: Full=Semenogelin I;
DE            Short=SGI;
DE   Contains:
DE     RecName: Full=Alpha-inhibin-92;
DE   Contains:
DE     RecName: Full=Alpha-inhibin-31;
DE   Contains:
DE     RecName: Full=Seminal basic protein;
DE   Flags: Precursor;
GN   Name=SEMG1; Synonyms=SEMG;
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] (ISOFORM 1), AND PYROGLUTAMATE FORMATION AT
RP   GLN-24.
RX   PubMed=2912989; DOI=10.1016/s0021-9258(18)94272-9;
RA   Lilja H., Abrahamsson P.-A., Lundwall A.;
RT   "Semenogelin, the predominant protein in human semen. Primary structure and
RT   identification of closely related proteins in the male accessory sex glands
RT   and on the spermatozoa.";
RL   J. Biol. Chem. 264:1894-1900(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=1517240; DOI=10.1016/s0021-9258(19)37155-8;
RA   Ulvsbaeck M., Lazure C., Lilja H., Spurr N.K., Rao V.V., Loeffler C.,
RA   Hansmann I., Lundwall A.;
RT   "Gene structure of semenogelin I and II. The predominant proteins in human
RT   semen are encoded by two homologous genes on chromosome 20.";
RL   J. Biol. Chem. 267:18080-18084(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-79 AND LEU-372.
RX   PubMed=14629036; DOI=10.1007/s00239-003-2474-x;
RA   Jensen-Seaman M.I., Li W.-H.;
RT   "Evolution of the hominoid semenogelin genes, the major proteins of
RT   ejaculated semen.";
RL   J. Mol. Evol. 57:261-270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, AND VARIANT
RP   THR-79.
RX   PubMed=14562960; DOI=10.1007/s00239-002-2463-0;
RA   Kingan S.B., Tatar M., Rand D.M.;
RT   "Reduced polymorphism in the chimpanzee semen coagulating protein,
RT   semenogelin I.";
RL   J. Mol. Evol. 57:159-169(2003).
RN   [9]
RP   PROTEIN SEQUENCE OF 108-159.
RX   PubMed=3972122; DOI=10.1016/0014-5793(85)81179-0;
RA   Lilja H., Jeppsson J.-O.;
RT   "Amino acid sequence of the predominant basic protein in human seminal
RT   plasma.";
RL   FEBS Lett. 182:181-184(1985).
RN   [10]
RP   PROTEIN SEQUENCE OF 108-138.
RX   PubMed=6698208; DOI=10.1016/0014-5793(84)80840-6;
RA   Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.;
RT   "Partial amino acid sequence of a human seminal plasma peptide with
RT   inhibin-like activity.";
RL   FEBS Lett. 167:98-102(1984).
RN   [11]
RP   PROTEIN SEQUENCE OF 108-138.
RX   PubMed=6422553; DOI=10.1126/science.6422553;
RA   Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P.,
RA   Schiller P.W., Yamashiro D., Li C.H.;
RT   "Isolation, structure, and synthesis of a human seminal plasma peptide with
RT   inhibin-like activity.";
RL   Science 223:1199-1202(1984).
RN   [12]
RP   PROTEIN SEQUENCE OF 316-344.
RX   PubMed=2757795;
RA   Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT   "Isolation and structure determination of two peptides occurring in human
RT   seminal plasma.";
RL   Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN   [13]
RP   PROTEIN SEQUENCE OF 373-397.
RX   PubMed=8444163; DOI=10.1111/j.1432-1033.1993.tb17629.x;
RA   Khan Z., Smyth D.G.;
RT   "Isolation and identification of N-terminally extended forms of 5-
RT   oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-releasing-
RT   hormone (TRH)-like peptide present in human semen.";
RL   Eur. J. Biochem. 212:35-40(1993).
RN   [14]
RP   PROTEIN SEQUENCE OF 68-159.
RX   PubMed=3889920; DOI=10.1073/pnas.82.12.4041;
RA   Li C.H., Hammonds R.G., Ramasharma K., Chung D.;
RT   "Human seminal alpha inhibins: isolation, characterization, and
RT   structure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985).
RN   [15]
RP   REVIEW.
RX   PubMed=10412373; DOI=10.1007/s000180050346;
RA   Robert M., Gagnon C.;
RT   "Semenogelin I: a coagulum forming, multifunctional seminal vesicle
RT   protein.";
RL   Cell. Mol. Life Sci. 55:944-960(1999).
RN   [16]
RP   INTERACTION WITH EPPIN.
RX   PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
RA   Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
RT   "Association of eppin with semenogelin on human spermatozoa.";
RL   Biol. Reprod. 72:1064-1070(2005).
RN   [17]
RP   IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
RX   PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
RA   Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT   "Characterization of an eppin protein complex from human semen and
RT   spermatozoa.";
RL   Biol. Reprod. 77:476-484(2007).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF CYS-239.
RX   PubMed=19889947; DOI=10.1095/biolreprod.109.081331;
RA   Mitra A., Richardson R.T., O'Rand M.G.;
RT   "Analysis of recombinant human semenogelin as an inhibitor of human sperm
RT   motility.";
RL   Biol. Reprod. 82:489-496(2010).
CC   -!- FUNCTION: Predominant protein in semen. It participates in the
CC       formation of a gel matrix entrapping the accessory gland secretions and
CC       ejaculated spermatozoa. Fragments of semenogelin and/or fragments of
CC       the related proteins may contribute to the activation of progressive
CC       sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.
CC       {ECO:0000269|PubMed:19889947}.
CC   -!- FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the
CC       proteolytic degradation of semenogelin, inhibit the secretion of
CC       pituitary follicle-stimulating hormone. {ECO:0000269|PubMed:19889947}.
CC   -!- SUBUNIT: Occurs in disulfide-linked complexes which may also contain
CC       two less abundant 71- and 76-kDa semenogelin-related polypeptides.
CC       Interacts with EPPIN (via C-terminus); Cys-239 is a critical amino acid
CC       for both binding to EPPIN. {ECO:0000269|PubMed:15590901,
CC       ECO:0000269|PubMed:17567961}.
CC   -!- INTERACTION:
CC       P04279-2; Q96JC9: EAF1; NbExp=3; IntAct=EBI-12272118, EBI-769261;
CC       P04279-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12272118, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P04279-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P04279-2; Sequence=VSP_004385;
CC   -!- TISSUE SPECIFICITY: Seminal vesicle.
CC   -!- PTM: Transglutaminase substrate.
CC   -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC       liquefaction of the semen coagulum and the progressive release of
CC       motile spermatozoa.
CC   -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue 62 of
CC       September 2005;
CC       URL="https://web.expasy.org/spotlight/back_issues/062";
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DR   EMBL; J04440; AAB59506.1; -; mRNA.
DR   EMBL; Z47556; CAA87636.1; -; Genomic_DNA.
DR   EMBL; M81650; AAA18168.1; -; Genomic_DNA.
DR   EMBL; AY256465; AAP82462.1; -; Genomic_DNA.
DR   EMBL; AY256466; AAP82463.1; -; Genomic_DNA.
DR   EMBL; AY256467; AAP82464.1; -; Genomic_DNA.
DR   EMBL; AY256468; AAP82465.1; -; Genomic_DNA.
DR   EMBL; AY256469; AAP82466.1; -; Genomic_DNA.
DR   EMBL; BT007177; AAP35841.1; -; mRNA.
DR   EMBL; AL049767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75871.1; -; Genomic_DNA.
DR   EMBL; BC007096; AAH07096.1; -; mRNA.
DR   EMBL; BC055416; AAH55416.1; -; mRNA.
DR   EMBL; AY174423; AAO20112.1; -; Genomic_DNA.
DR   EMBL; AY174424; AAO20113.1; -; Genomic_DNA.
DR   EMBL; AY174437; AAO20126.1; -; Genomic_DNA.
DR   CCDS; CCDS13345.1; -. [P04279-1]
DR   PIR; B43412; WTHUB.
DR   RefSeq; NP_002998.1; NM_003007.4. [P04279-1]
DR   PDB; 7ZRF; NMR; -; A=68-85.
DR   PDB; 7ZRO; NMR; -; A=68-107.
DR   PDB; 8BOO; NMR; -; A=45-67.
DR   PDB; 8BVZ; NMR; -; A=49-67.
DR   PDBsum; 7ZRF; -.
DR   PDBsum; 7ZRO; -.
DR   PDBsum; 8BOO; -.
DR   PDBsum; 8BVZ; -.
DR   AlphaFoldDB; P04279; -.
DR   SMR; P04279; -.
DR   BioGRID; 112306; 109.
DR   IntAct; P04279; 32.
DR   MINT; P04279; -.
DR   STRING; 9606.ENSP00000361867; -.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   iPTMnet; P04279; -.
DR   PhosphoSitePlus; P04279; -.
DR   BioMuta; SEMG1; -.
DR   DMDM; 134426; -.
DR   jPOST; P04279; -.
DR   MassIVE; P04279; -.
DR   MaxQB; P04279; -.
DR   PaxDb; 9606-ENSP00000361867; -.
DR   PeptideAtlas; P04279; -.
DR   ProteomicsDB; 51699; -. [P04279-1]
DR   ProteomicsDB; 51700; -. [P04279-2]
DR   Pumba; P04279; -.
DR   Antibodypedia; 12686; 262 antibodies from 29 providers.
DR   DNASU; 6406; -.
DR   Ensembl; ENST00000372781.4; ENSP00000361867.3; ENSG00000124233.12. [P04279-1]
DR   GeneID; 6406; -.
DR   KEGG; hsa:6406; -.
DR   MANE-Select; ENST00000372781.4; ENSP00000361867.3; NM_003007.5; NP_002998.1.
DR   UCSC; uc002xni.3; human. [P04279-1]
DR   AGR; HGNC:10742; -.
DR   CTD; 6406; -.
DR   DisGeNET; 6406; -.
DR   GeneCards; SEMG1; -.
DR   HGNC; HGNC:10742; SEMG1.
DR   HPA; ENSG00000124233; Tissue enriched (seminal).
DR   MIM; 182140; gene.
DR   neXtProt; NX_P04279; -.
DR   OpenTargets; ENSG00000124233; -.
DR   PharmGKB; PA35664; -.
DR   VEuPathDB; HostDB:ENSG00000124233; -.
DR   eggNOG; ENOG502T80H; Eukaryota.
DR   GeneTree; ENSGT00940000162560; -.
DR   HOGENOM; CLU_034710_0_0_1; -.
DR   InParanoid; P04279; -.
DR   OMA; QRHNYDR; -.
DR   OrthoDB; 4729048at2759; -.
DR   PhylomeDB; P04279; -.
DR   TreeFam; TF342360; -.
DR   PathwayCommons; P04279; -.
DR   Reactome; R-HSA-6803157; Antimicrobial peptides.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P04279; -.
DR   BioGRID-ORCS; 6406; 11 hits in 1135 CRISPR screens.
DR   ChiTaRS; SEMG1; human.
DR   GeneWiki; Semenogelin_I; -.
DR   GenomeRNAi; 6406; -.
DR   Pharos; P04279; Tbio.
DR   PRO; PR:P04279; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P04279; Protein.
DR   Bgee; ENSG00000124233; Expressed in seminal vesicle and 65 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0050817; P:coagulation; IDA:UniProtKB.
DR   GO; GO:0007320; P:insemination; TAS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IDA:CACAO.
DR   GO; GO:1901318; P:negative regulation of flagellated sperm motility; IDA:CACAO.
DR   GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR   InterPro; IPR008836; Semenogelin.
DR   PANTHER; PTHR10547:SF4; SEMENOGELIN-1; 1.
DR   PANTHER; PTHR10547; SEMENOGELIN/SEMINAL VESICLE SECRETORY PROTEIN; 1.
DR   Pfam; PF05474; Semenogelin; 2.
DR   Genevisible; P04279; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..462
FT                   /note="Semenogelin-1"
FT                   /id="PRO_0000032351"
FT   PEPTIDE         68..159
FT                   /note="Alpha-inhibin-92"
FT                   /id="PRO_0000032352"
FT   PEPTIDE         108..159
FT                   /note="Seminal basic protein"
FT                   /id="PRO_0000032353"
FT   PEPTIDE         108..138
FT                   /note="Alpha-inhibin-31"
FT                   /id="PRO_0000032354"
FT   REPEAT          70..129
FT                   /note="3-1"
FT   REPEAT          141..200
FT                   /note="2-1"
FT   REPEAT          201..260
FT                   /note="2-2"
FT   REPEAT          381..439
FT                   /note="3-2"
FT   REGION          24..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..439
FT                   /note="Repeat-rich region"
FT                   /evidence="ECO:0000250"
FT   REGION          131..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..283
FT                   /note="Interaction with EPPIN"
FT                   /evidence="ECO:0000269|PubMed:15590901"
FT   REGION          173..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..380
FT                   /note="2 X 60 AA tandem repeats, type 1"
FT   REGION          270..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:2912989"
FT   DISULFID        239
FT                   /note="Interchain"
FT   VAR_SEQ         312..371
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT                   /id="VSP_004385"
FT   VARIANT         58
FT                   /note="E -> G (in dbSNP:rs11559137)"
FT                   /id="VAR_053650"
FT   VARIANT         79
FT                   /note="S -> T (less common genetic variant;
FT                   dbSNP:rs2301366)"
FT                   /evidence="ECO:0000269|PubMed:14562960,
FT                   ECO:0000269|PubMed:14629036"
FT                   /id="VAR_005610"
FT   VARIANT         108
FT                   /note="H -> R (in dbSNP:rs2233884)"
FT                   /id="VAR_053651"
FT   VARIANT         372
FT                   /note="R -> L (in dbSNP:rs2233887)"
FT                   /evidence="ECO:0000269|PubMed:14629036"
FT                   /id="VAR_022679"
FT   MUTAGEN         239
FT                   /note="C->G: Abrogates binding to EPPIN and do not inhibit
FT                   spem motility."
FT                   /evidence="ECO:0000269|PubMed:19889947"
FT   CONFLICT        100
FT                   /note="L -> Q (in Ref. 3; AAP82463)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235..237
FT                   /note="QTS -> LRT (in Ref. 8; AAO20112/AAO20113)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="K -> L (in Ref. 12; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="K -> N (in Ref. 2; CAA87636/AAA18168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        457
FT                   /note="R -> Q (in Ref. 4 and 7)"
FT                   /evidence="ECO:0000305"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:7ZRF"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:7ZRO"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:7ZRO"
SQ   SEQUENCE   462 AA;  52131 MW;  760F48EFCF2FA702 CRC64;
     MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK
     GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK
     GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG
     AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP
     AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY
     GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY
     GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH
     EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT
//