ID   CRIS_PROFL              Reviewed;         221 AA.
AC   P0CB15;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Serotriflin;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-39, SUBUNIT WITH SSP-2,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver, and Serum;
RX   PubMed=18222185; DOI=10.1016/j.bbapap.2007.12.010;
RA   Aoki N., Sakiyama A., Kuroki K., Maenaka K., Kohda D., Deshimaru M.,
RA   Terada S.;
RT   "Serotriflin, a CRISP family protein with binding affinity for small serum
RT   protein-2 in snake serum.";
RL   Biochim. Biophys. Acta 1784:621-628(2008).
CC   -!- SUBUNIT: Forms a stable, non-covalent complex with SSP-2.
CC       {ECO:0000269|PubMed:18222185}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=27645.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18222185};
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CB15; -.
DR   SMR; P0CB15; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   CDD; cd05383; CAP_CRISP; 1.
DR   Gene3D; 1.10.10.740; -; 1.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR042076; Crisp-like_dom.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR013871; Cysteine_rich_secretory.
DR   InterPro; IPR034117; SCP_CRISP.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted.
FT   CHAIN           1..221
FT                   /note="Serotriflin"
FT                   /id="PRO_0000380641"
FT   DOMAIN          19..147
FT                   /note="SCP"
FT   DOMAIN          183..216
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        73..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        129..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        167..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        170..179
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        183..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        192..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        201..214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   221 AA;  24899 MW;  05BDEE668DFFF259 CRC64;
     TVDFASESAN ERETQKEILD KHNALRRSVR PTARNMLQME WNFNAAQNAT RWADRCSFAH
     SPQHLRTVGE LKCGENLFMS SHPFPWTRVI QSWYDENKNF KYGVGANPPN AVIGHYTQIV
     WYKSYLLGCA AARCPSSSYN YYYVCHYCPA GNIIGKIATP YKSGPPCGDC PSACVNGLCT
     NPCKHVDRYS NCNSLVQQIS CQSNNMNTDC PASCFCHNEI K