ISK13_HUMAN
ID ISK13_HUMAN Reviewed; 94 AA.
AC Q1W4C9; A1A4Y2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Serine protease inhibitor Kazal-type 13;
DE AltName: Full=Hepatitis B virus DNA polymerase transactivated serine protease inhibitor;
DE AltName: Full=Hespintor;
DE AltName: Full=Serine protease inhibitor Kazal-type 5-like 3;
DE Flags: Precursor;
GN Name=SPINK13; Synonyms=HBVDNAPTP1, SPINK5L3;
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).
RA Lun Y.Z., Yu Z.G., Cheng J.;
RT "Gene cloning and bioinformatics analysis of human hespintor: a novel
RT serine protease inhibitor.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
CC -!- FUNCTION: May be a serine protease inhibitor (By similarity). Essential
CC for sperm maturation and fertility. Inhibits sperm acrosome reaction,
CC protecting sperm from premature reaction (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q1W4C9; P42858: HTT; NbExp=3; IntAct=EBI-25953827, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted into the
CC lumen of the initial segment of the epididymis and binds to sperm. In
CC the initial segment of epididymis, localizes on the dorsal surface of
CC the acrosomal region of sperm, gradually becomes more restricted to the
CC acrosomal region in spermatozoa during epididymal transit (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1W4C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1W4C9-2; Sequence=VSP_034842;
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DR EMBL; DQ438947; ABD96086.1; -; mRNA.
DR EMBL; CH471062; EAW61812.1; -; Genomic_DNA.
DR EMBL; BC128163; AAI28164.1; -; mRNA.
DR EMBL; BC128164; AAI28165.1; -; mRNA.
DR CCDS; CCDS43383.1; -. [Q1W4C9-1]
DR RefSeq; NP_001035218.1; NM_001040129.2. [Q1W4C9-1]
DR AlphaFoldDB; Q1W4C9; -.
DR SMR; Q1W4C9; -.
DR IntAct; Q1W4C9; 1.
DR STRING; 9606.ENSP00000421048; -.
DR GlyGen; Q1W4C9; 1 site.
DR iPTMnet; Q1W4C9; -.
DR PhosphoSitePlus; Q1W4C9; -.
DR BioMuta; SPINK13; -.
DR DMDM; 121940862; -.
DR MassIVE; Q1W4C9; -.
DR PaxDb; Q1W4C9; -.
DR PeptideAtlas; Q1W4C9; -.
DR PRIDE; Q1W4C9; -.
DR Antibodypedia; 49010; 14 antibodies from 7 providers.
DR DNASU; 153218; -.
DR Ensembl; ENST00000398450.5; ENSP00000381468.4; ENSG00000214510.10. [Q1W4C9-1]
DR Ensembl; ENST00000511106.5; ENSP00000426279.1; ENSG00000214510.10. [Q1W4C9-2]
DR Ensembl; ENST00000512953.5; ENSP00000421048.1; ENSG00000214510.10. [Q1W4C9-1]
DR GeneID; 153218; -.
DR KEGG; hsa:153218; -.
DR MANE-Select; ENST00000398450.5; ENSP00000381468.4; NM_001040129.3; NP_001035218.1.
DR UCSC; uc003lpc.4; human. [Q1W4C9-1]
DR CTD; 153218; -.
DR DisGeNET; 153218; -.
DR GeneCards; SPINK13; -.
DR HGNC; HGNC:27200; SPINK13.
DR HPA; ENSG00000214510; Tissue enriched (epididymis).
DR MIM; 615205; gene.
DR neXtProt; NX_Q1W4C9; -.
DR OpenTargets; ENSG00000214510; -.
DR PharmGKB; PA165660568; -.
DR VEuPathDB; HostDB:ENSG00000214510; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00400000023784; -.
DR HOGENOM; CLU_161738_0_0_1; -.
DR InParanoid; Q1W4C9; -.
DR OMA; FFCVEQW; -.
DR OrthoDB; 1550974at2759; -.
DR PhylomeDB; Q1W4C9; -.
DR PathwayCommons; Q1W4C9; -.
DR SignaLink; Q1W4C9; -.
DR BioGRID-ORCS; 153218; 9 hits in 1023 CRISPR screens.
DR GenomeRNAi; 153218; -.
DR Pharos; Q1W4C9; Tdark.
DR PRO; PR:Q1W4C9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q1W4C9; protein.
DR Bgee; ENSG00000214510; Expressed in corpus epididymis and 95 other tissues.
DR Genevisible; Q1W4C9; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:1902225; P:negative regulation of acrosome reaction; ISS:UniProtKB.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF00050; Kazal_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..94
FT /note="Serine protease inhibitor Kazal-type 13"
FT /id="PRO_0000344510"
FT DOMAIN 33..94
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 55..56
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 53..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 61..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034842"
SQ SEQUENCE 94 AA; 11051 MW; 120BA36AD5A8B79F CRC64;
MAAFPHKIIF FLVCSTLTHV AFSGIFNKRD FTRWPKPRCK MYIPLDPDYN ADCPNVTAPV
CASNGHTFQN ECFFCVEQRE FHYRIKFEKY GKCD