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Database: UniProt
Entry: A0A7K9Y4Q4_9GALL
LinkDB: A0A7K9Y4Q4_9GALL
Original site: A0A7K9Y4Q4_9GALL 
ID   A0A7K9Y4Q4_9GALL        Unreviewed;       448 AA.
AC   A0A7K9Y4Q4;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 16.
DE   RecName: Full=Transmembrane protease serine 5 {ECO:0000256|ARBA:ARBA00071705};
DE   AltName: Full=Spinesin {ECO:0000256|ARBA:ARBA00075021};
DE   Flags: Fragment;
GN   Name=Tmprss5 {ECO:0000313|EMBL:NXJ04618.1};
GN   ORFNames=ODOGUJ_R11045 {ECO:0000313|EMBL:NXJ04618.1};
OS   Odontophorus gujanensis (marbled wood quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Odontophorus.
OX   NCBI_TaxID=886794 {ECO:0000313|EMBL:NXJ04618.1, ECO:0000313|Proteomes:UP000522663};
RN   [1] {ECO:0000313|EMBL:NXJ04618.1, ECO:0000313|Proteomes:UP000522663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B10K-DU-001-53 {ECO:0000313|EMBL:NXJ04618.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXJ04618.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in hearing. {ECO:0000256|ARBA:ARBA00056576}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NXJ04618.1}.
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DR   EMBL; VXAB01001531; NXJ04618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7K9Y4Q4; -.
DR   OrthoDB; 5979691at2759; -.
DR   Proteomes; UP000522663; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000092; Transmembrane protease serine 5; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001190; SRCR.
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:SF17; SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN HOMOLOG-RELATED; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
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   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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|ARBA:ARBA00023136};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000522663};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          77..172
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          210..444
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          49..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..199
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXJ04618.1"
FT   NON_TER         448
FT                   /evidence="ECO:0000313|EMBL:NXJ04618.1"
SQ   SEQUENCE   448 AA;  48043 MW;  89952FE6229D1EA2 CRC64;
     SSNASPKTLC TTWRLLLLLL LGGSGLLAAA VAGAWLLGQH LGGSQPQQVL AKPQALDPGT
     ACSEGEEEEP VVRGAPGRVS FRIQAGPSLL AVRPWELSQW LLACHERWQP TLGTRLCRHL
     GALRAIHQKG VNLTDVEVED GQRFAQVGSS LEDAWQVRSS CESGRVVALQ CSGGSLSLHY
     LSPAASSPSH PLSPGSAAAC GQRPAPGGRV VGGTDAAPGR WPWQVSVRLG SRHRCGGSVL
     APRWIVTAAH CVHSYRRRSA WGWMIHAGIT HGSAKQEDGV PVERVISHPL YNDSSLDYDI
     ALMKLQVPLN FSDAISALCL LPSHQDLLPG TPCWVSGWGY TRPDQAQLTE TLKEALVPLI
     STQRCNSSCM YAGELTARML CAGYPQGKVD ACQGDSGGPL VCRDELAWRL VGIVSWGRGC
     AEPNRPGVYT NVAQLLPWIY RVTEVRCS
//
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