INSL3_HUMAN
ID INSL3_HUMAN Reviewed; 131 AA.
AC P51460; B4DZ72; G3XAG0; Q3KPI5; Q3KPI6; Q6YNB5; Q9UEA2; Q9UPH6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Insulin-like 3;
DE AltName: Full=Leydig insulin-like peptide;
DE Short=Ley-I-L;
DE AltName: Full=Relaxin-like factor;
DE Contains:
DE RecName: Full=Insulin-like 3 B chain;
DE Contains:
DE RecName: Full=Insulin-like 3 A chain;
DE Flags: Precursor;
GN Name=INSL3; Synonyms=RLF, RLNL;
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 VARIANT ALA-60.
RC TISSUE=Testis;
RX PubMed=8034302; DOI=10.1007/bf02272850;
RA Burkhardt E., Adham I.M., Hobohm U., Murphy D., Sander C., Engel W.;
RT "A human cDNA coding for the Leydig insulin-like peptide (Ley I-L).";
RL Hum. Genet. 94:91-94(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-60.
RX PubMed=8020942; DOI=10.1006/geno.1994.1121;
RA Burkhardt E., Adham I.M., Brosig B., Gastmann A., Mattei M.-G., Engel W.;
RT "Structural organization of the porcine and human genes coding for a Leydig
RT cell-specific insulin-like peptide (LEY I-L) and chromosomal localization
RT of the human gene (INSL3).";
RL Genomics 20:13-19(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=7852540; DOI=10.1210/jcem.80.2.7852540;
RA Tashima L.S., Hieber A.D., Greenwood F.C., Bryant-Greenwood G.D.;
RT "The human Leydig insulin-like (hLEY I-L) gene is expressed in the corpus
RT luteum and trophoblast.";
RL J. Clin. Endocrinol. Metab. 80:707-710(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Lim H.N., Oakenfull E.A., Rajpert De Meyts E., Skakkebaek N.E.,
RA Hughes I.A., Hawkins J.R., Farr C.J.;
RT "A novel human relaxin-like factor: evidence for the evolution of new
RT hormonal functions?";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-60.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-60.
RC TISSUE=Brain;
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 [9]
RP PROTEIN SEQUENCE OF 21-35.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [10]
RP INTERACTION WITH LGR8.
RX PubMed=12114498; DOI=10.1074/jbc.c200398200;
RA Kumagai J., Hsu S.Y., Matsumi H., Roh J.-S., Fu P., Wade J.D.,
RA Bathgate R.A.D., Hsueh A.J.W.;
RT "INSL3/Leydig insulin-like peptide activates the LGR8 receptor important in
RT testis descent.";
RL J. Biol. Chem. 277:31283-31286(2002).
RN [11]
RP STRUCTURE BY NMR OF 25-55 AND 106-131, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=16867980; DOI=10.1074/jbc.m603829200;
RA Rosengren K.J., Zhang S., Lin F., Daly N.L., Scott D.J., Hughes R.A.,
RA Bathgate R.A., Craik D.J., Wade J.D.;
RT "Solution structure and characterization of the LGR8 receptor binding
RT surface of insulin-like peptide 3.";
RL J. Biol. Chem. 281:28287-28295(2006).
RN [12]
RP STRUCTURE BY NMR OF 25-55 AND 106-131, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=19086273; DOI=10.1021/bi801412w;
RA Bullesbach E.E., Hass M.A., Jensen M.R., Hansen D.F., Kristensen S.M.,
RA Schwabe C., Led J.J.;
RT "Solution structure of a conformationally restricted fully active
RT derivative of the human relaxin-like factor.";
RL Biochemistry 47:13308-13317(2008).
RN [13]
RP VARIANT ALA-60.
RX PubMed=10729310; DOI=10.1093/molehr/6.4.298;
RA Krausz C., Quintana-Murci L., Fellous M., Siffroi J.P., McElreavey K.;
RT "Absence of mutations involving the INSL3 gene in human idiopathic
RT cryptorchidism.";
RL Mol. Hum. Reprod. 6:298-302(2000).
RN [14]
RP VARIANT CRYPTO LEU-93, AND VARIANT ALA-60.
RX PubMed=11095425; DOI=10.1210/jcem.85.11.6935;
RA Tomboc M., Lee P.A., Mitwally M.F., Schneck F.X., Bellinger M.,
RA Witchel S.F.;
RT "Insulin-like 3/relaxin-like factor gene mutations are associated with
RT cryptorchidism.";
RL J. Clin. Endocrinol. Metab. 85:4013-4018(2000).
RN [15]
RP VARIANT ALA-60.
RX PubMed=10759163; DOI=10.1203/00006450-200004000-00020;
RA Koskimies P., Virtanen H., Lindstroem M., Kaleva M., Poutanen M.,
RA Huhtaniemi I., Toppari J.;
RT "A common polymorphism in the human relaxin-like factor (RLF) gene: no
RT relationship with cryptorchidism.";
RL Pediatr. Res. 47:538-541(2000).
RN [16]
RP VARIANT CRYPTO CYS-102, AND VARIANT ALA-60.
RX PubMed=11746019; DOI=10.1002/ajmg.1579.abs;
RA Marin P., Ferlin A., Moro E., Rossi A., Bartoloni L., Rossato M.,
RA Foresta C.;
RT "Novel insulin-like 3 (INSL3) gene mutation associated with human
RT cryptorchidism.";
RL Am. J. Med. Genet. 103:348-349(2001).
RN [17]
RP VARIANTS GLY-24; LEU-43; SER-49; ALA-60 AND HIS-102.
RX PubMed=11182749; DOI=10.1530/eje.0.1440129;
RA Lim H.N., Raipert-de Meyts E., Skakkebaek N.E., Hawkins J.R., Hughes I.A.;
RT "Genetic analysis of the INSL3 gene in patients with maldescent of the
RT testis.";
RL Eur. J. Endocrinol. 144:129-137(2001).
RN [18]
RP VARIANT ALA-60.
RX PubMed=11383919; DOI=10.1007/bf03343848;
RA Marin P., Ferlin A., Moro E., Garolla A., Foresta C.;
RT "Different insulin-like 3 (INSL3) gene mutations not associated with human
RT cryptorchidism.";
RL J. Endocrinol. Invest. 24:RC13-RC15(2001).
RN [19]
RP VARIANT ALA-60.
RX PubMed=11380919; DOI=10.1046/j.1442-200x.2001.01390.x;
RA Takahashi I., Takahashi T., Komatsu M., Matsuda J., Takada G.;
RT "Ala/Thr60 variant of the Leydig insulin-like hormone is not associated
RT with cryptorchidism in the Japanese population.";
RL Pediatr. Int. 43:256-258(2001).
RN [20]
RP VARIANT CRYPTO LYS-110.
RX PubMed=12601553; DOI=10.1007/s100380300012;
RA Canto P., Escudero I., Soederlund D., Nishimura E., Carranza-Lira S.,
RA Gutierrez J., Nava A., Mendez J.P.;
RT "A novel mutation of the insulin-like 3 gene in patients with
RT cryptorchidism.";
RL J. Hum. Genet. 48:86-90(2003).
CC -!- FUNCTION: Seems to play a role in testicular function. May be a trophic
CC hormone with a role in testicular descent in fetal life. Is a ligand
CC for LGR8 receptor.
CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC disulfide bonds. {ECO:0000269|PubMed:16867980,
CC ECO:0000269|PubMed:19086273}.
CC -!- INTERACTION:
CC P51460; Q99622: C12orf57; NbExp=3; IntAct=EBI-12919766, EBI-2808472;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51460-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51460-2; Sequence=VSP_045526;
CC -!- TISSUE SPECIFICITY: Expressed in prenatal and postnatal Leydig cells.
CC Found as well in the corpus luteum, trophoblast, fetal membranes and
CC breast. {ECO:0000269|PubMed:7852540}.
CC -!- DISEASE: Cryptorchidism (CRYPTO) [MIM:219050]: One of the most frequent
CC congenital abnormalities in humans, involving 2-5% of male births.
CC Cryptorchidism is associated with increased risk of infertility and
CC testicular cancer. {ECO:0000269|PubMed:11095425,
CC ECO:0000269|PubMed:11746019, ECO:0000269|PubMed:12601553}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S72482; AAB31371.1; -; mRNA.
DR EMBL; X73637; CAA52017.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY082014; AAL92559.1; -; mRNA.
DR EMBL; AK302780; BAG63984.1; -; mRNA.
DR EMBL; AC005952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007201; AAD22740.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84635.1; -; Genomic_DNA.
DR EMBL; BC032810; AAH32810.1; -; mRNA.
DR EMBL; BC053345; AAH53345.1; -; mRNA.
DR EMBL; BC071706; AAH71706.1; -; mRNA.
DR EMBL; BC106721; AAI06722.1; -; mRNA.
DR EMBL; BC106722; AAI06723.1; -; mRNA.
DR CCDS; CCDS12365.1; -. [P51460-1]
DR CCDS; CCDS58655.1; -. [P51460-2]
DR PIR; B53024; B53024.
DR RefSeq; NP_001252516.1; NM_001265587.1. [P51460-2]
DR RefSeq; NP_005534.2; NM_005543.3. [P51460-1]
DR PDB; 2H8B; NMR; -; A=106-131, B=25-55.
DR PDB; 2K6T; NMR; -; A=106-131, B=25-55.
DR PDB; 2K6U; NMR; -; A=106-131, B=25-49.
DR PDBsum; 2H8B; -.
DR PDBsum; 2K6T; -.
DR PDBsum; 2K6U; -.
DR AlphaFoldDB; P51460; -.
DR BMRB; P51460; -.
DR SMR; P51460; -.
DR BioGRID; 109851; 21.
DR IntAct; P51460; 8.
DR STRING; 9606.ENSP00000369017; -.
DR BioMuta; INSL3; -.
DR DMDM; 317373369; -.
DR MassIVE; P51460; -.
DR PaxDb; P51460; -.
DR PeptideAtlas; P51460; -.
DR PRIDE; P51460; -.
DR ProteomicsDB; 56309; -. [P51460-1]
DR Antibodypedia; 35351; 195 antibodies from 27 providers.
DR DNASU; 3640; -.
DR Ensembl; ENST00000317306.8; ENSP00000321724.6; ENSG00000248099.4. [P51460-1]
DR Ensembl; ENST00000379695.5; ENSP00000369017.4; ENSG00000248099.4. [P51460-2]
DR GeneID; 3640; -.
DR KEGG; hsa:3640; -.
DR MANE-Select; ENST00000317306.8; ENSP00000321724.6; NM_005543.4; NP_005534.2.
DR UCSC; uc002nhm.3; human. [P51460-1]
DR CTD; 3640; -.
DR DisGeNET; 3640; -.
DR GeneCards; INSL3; -.
DR HGNC; HGNC:6086; INSL3.
DR HPA; ENSG00000248099; Tissue enriched (testis).
DR MalaCards; INSL3; -.
DR MIM; 146738; gene.
DR MIM; 219050; phenotype.
DR neXtProt; NX_P51460; -.
DR OpenTargets; ENSG00000248099; -.
DR PharmGKB; PA29893; -.
DR VEuPathDB; HostDB:ENSG00000248099; -.
DR eggNOG; ENOG502TFQJ; Eukaryota.
DR GeneTree; ENSGT00940000163613; -.
DR HOGENOM; CLU_164865_0_0_1; -.
DR InParanoid; P51460; -.
DR OMA; NPAHHCC; -.
DR OrthoDB; 1365119at2759; -.
DR PhylomeDB; P51460; -.
DR TreeFam; TF106361; -.
DR PathwayCommons; P51460; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-444821; Relaxin receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P51460; -.
DR BioGRID-ORCS; 3640; 12 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; P51460; -.
DR GeneWiki; INSL3; -.
DR GenomeRNAi; 3640; -.
DR Pharos; P51460; Tbio.
DR PRO; PR:P51460; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P51460; protein.
DR Bgee; ENSG00000248099; Expressed in adult organism and 108 other tissues.
DR ExpressionAtlas; P51460; baseline and differential.
DR Genevisible; P51460; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; TAS:ProtInc.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:CACAO.
DR GO; GO:0090303; P:positive regulation of wound healing; IDA:CACAO.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR InterPro; IPR040113; INSL3.
DR InterPro; IPR043387; INSL3/INSL4.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR PANTHER; PTHR10423; PTHR10423; 1.
DR PANTHER; PTHR10423:SF6; PTHR10423:SF6; 1.
DR Pfam; PF00049; Insulin; 1.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disease variant; Disulfide bond; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15340161"
FT PEPTIDE 21..55
FT /note="Insulin-like 3 B chain"
FT /id="PRO_0000016140"
FT PROPEP 58..104
FT /note="C peptide like"
FT /evidence="ECO:0000255"
FT /id="PRO_0000016141"
FT PEPTIDE 106..131
FT /note="Insulin-like 3 A chain"
FT /id="PRO_0000016142"
FT DISULFID 34..116
FT /note="Interchain (between B and A chains)"
FT DISULFID 46..129
FT /note="Interchain (between B and A chains)"
FT DISULFID 115..120
FT VAR_SEQ 64..131
FT /note="RELLQWLERRHLLHGLVADSNLTLGPGLQPLPQTSHHHRHHRAAATNPARYC
FT CLSGCTQQDLLTLCPY -> QRESHSVSQAGLKLLSSSNPPTLTFQSVGISDVSCYSGW
FT RDDICSMGWWPTVISRWDLACSPCPRPLTITATTVQLPPTLHATAASVAVPNKTC (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045526"
FT VARIANT 24
FT /note="A -> G (in dbSNP:rs186828508)"
FT /evidence="ECO:0000269|PubMed:11182749"
FT /id="VAR_013231"
FT VARIANT 43
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:11182749"
FT /id="VAR_013232"
FT VARIANT 49
FT /note="P -> S (found in a male with undermasculinised
FT genitalia and intra-abdominal testes; unknown pathological
FT significance; dbSNP:rs751299877)"
FT /evidence="ECO:0000269|PubMed:11182749"
FT /id="VAR_013233"
FT VARIANT 60
FT /note="T -> A (in dbSNP:rs6523)"
FT /evidence="ECO:0000269|PubMed:10729310,
FT ECO:0000269|PubMed:10759163, ECO:0000269|PubMed:11095425,
FT ECO:0000269|PubMed:11182749, ECO:0000269|PubMed:11380919,
FT ECO:0000269|PubMed:11383919, ECO:0000269|PubMed:11746019,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8020942, ECO:0000269|PubMed:8034302"
FT /id="VAR_013234"
FT VARIANT 93
FT /note="P -> L (in CRYPTO; dbSNP:rs104894697)"
FT /evidence="ECO:0000269|PubMed:11095425"
FT /id="VAR_013235"
FT VARIANT 102
FT /note="R -> C (in CRYPTO; dbSNP:rs104894698)"
FT /evidence="ECO:0000269|PubMed:11746019"
FT /id="VAR_013236"
FT VARIANT 102
FT /note="R -> H (in dbSNP:rs121912556)"
FT /evidence="ECO:0000269|PubMed:11182749"
FT /id="VAR_013237"
FT VARIANT 110
FT /note="N -> K (in CRYPTO; dbSNP:rs121912555)"
FT /evidence="ECO:0000269|PubMed:12601553"
FT /id="VAR_017122"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:2H8B"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2H8B"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:2H8B"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:2H8B"
SQ SEQUENCE 131 AA; 14502 MW; 94788D700524C12A CRC64;
MDPRLPAWAL VLLGPALVFA LGPAPTPEMR EKLCGHHFVR ALVRVCGGPR WSTEARRPAT
GGDRELLQWL ERRHLLHGLV ADSNLTLGPG LQPLPQTSHH HRHHRAAATN PARYCCLSGC
TQQDLLTLCP Y
