ID   ISK2_MACFA              Reviewed;          81 AA.
AC   P34953;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Serine protease inhibitor Kazal-type 2;
DE   AltName: Full=Acrosin-trypsin inhibitor;
DE   Flags: Precursor;
GN   Name=SPINK2;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=8439554; DOI=10.1016/0167-4781(93)90284-k;
RA   Perry A.C.F., Jones R., Hall L.;
RT   "Sequence analysis of monkey acrosin-trypsin inhibitor transcripts and
RT   their abundant expression in the epididymis.";
RL   Biochim. Biophys. Acta 1172:159-160(1993).
CC   -!- FUNCTION: Strong inhibitor of acrosin in male and/or female genital
CC       tract. Also inhibits trypsin (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: As a strong inhibitor of acrosin, it is required for normal
CC       spermiogenesis. It probably hinders premature activation of proacrosin
CC       and other proteases, thus preventing the cascade of events leading to
CC       spermiogenesis defects (By similarity). May be involved in the
CC       regulation of serine protease-dependent germ cell apoptosis (By
CC       similarity). It also inhibits trypsin (By similarity).
CC       {ECO:0000250|UniProtKB:P20155, ECO:0000250|UniProtKB:Q8BMY7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20155}.
CC       Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:P20155}.
CC   -!- TISSUE SPECIFICITY: More abundant in epididymis than in testis.
CC       {ECO:0000269|PubMed:8439554}.
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DR   EMBL; X68331; CAA48408.1; -; mRNA.
DR   PIR; S29820; S29820.
DR   RefSeq; XP_005555275.1; XM_005555218.2.
DR   AlphaFoldDB; P34953; -.
DR   SMR; P34953; -.
DR   MEROPS; I01.012; -.
DR   GeneID; 102117158; -.
DR   KEGG; mcf:102117158; -.
DR   CTD; 6691; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB.
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:0001675; P:acrosome assembly; ISS:UniProtKB.
DR   GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR042167; SPINK2.
DR   PANTHER; PTHR47608; PTHR47608; 1.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS00282; KAZAL_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..81
FT                   /note="Serine protease inhibitor Kazal-type 2"
FT                   /id="PRO_0000016562"
FT   DOMAIN          27..81
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            43..44
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        33..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        41..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        49..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   81 AA;  9171 MW;  C506681D971F62B7 CRC64;
     MALAVLRLAL LLLAVTFAGP LFRRFSKYKT PFCARYQLPG CPRDFNPVCG TDMITYPNEC
     TLCMKIRESG QNIKILRRGP C