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Database: UniProt
Entry: H9GCR0_ANOCA
LinkDB: H9GCR0_ANOCA
Original site: H9GCR0_ANOCA 
ID   H9GCR0_ANOCA            Unreviewed;       481 AA.
AC   H9GCR0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSACAP00000007360.4};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007360.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000007360.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007360.4};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000007360.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.
CC       {ECO:0000256|ARBA:ARBA00009228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   AlphaFoldDB; H9GCR0; -.
DR   STRING; 28377.ENSACAP00000007360; -.
DR   MEROPS; S01.087; -.
DR   Ensembl; ENSACAT00000007516.4; ENSACAP00000007360.4; ENSACAG00000007471.4.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000159197; -.
DR   HOGENOM; CLU_006842_19_2_1; -.
DR   TreeFam; TF351678; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000007471; Expressed in kidney and 8 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0035821; P:modulation of process of another organism; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF14; TRANSMEMBRANE PROTEASE SERINE 3-LIKE; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        81..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          151..244
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          241..477
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   481 AA;  52858 MW;  DA02E8096A799FC1 CRC64;
     MQQAWRKGRR QAWKAHVAAS SPSSSIRAQT QAGLFLATAG AQCMILRDTW PKSSSGFGEK
     GAKDAGPPLL QLRAGMGRKR VALIACLLVL IALLLALILL FLFWRSGTDM VYKEPAETCK
     APVVRCDGTP DCSLKSDELD CVRFNWNGSL LRVFSAAEQE WLPVCSQDWT AAFAQKTCQQ
     LGFGNVSETD SVTLSHSGKS LLPAALKDTI QQSLNRTSEC PSRRYVTLRC SSCGQRLSGR
     IVEGAEAPSS KWPWQISLQY GSSHICGGTL LDPLWVLTAA HCFFMNNVKI LDRWKVVAGA
     SDLKRPGGGW EGVPVKEVII NANYSEEHDD YDIALLKLAR PLVLSAQVRP ACLPMSGQNF
     KPGRTCFITG YGKVNEHEEN TSPKLREAAV EIIDFRLCNR PSVYEGFLTP RMMCAGYLQG
     GRDSCQGDSG GPLVCEDGNR WYLAGVTSWG TGCGQKDKPG VYTQVNKMLS WIYSKMESQR
     H
//
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