ID A0A091PSB3_HALAL Unreviewed; 594 AA.
AC A0A091PSB3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Inactive serine protease PAMR1 {ECO:0000256|ARBA:ARBA00040464};
DE AltName: Full=Peptidase domain-containing protein associated with muscle regeneration 1 {ECO:0000256|ARBA:ARBA00042985};
DE AltName: Full=Regeneration-associated muscle protease homolog {ECO:0000256|ARBA:ARBA00041872};
DE Flags: Fragment;
GN ORFNames=N329_01568 {ECO:0000313|EMBL:KFQ10565.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ10565.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFQ10565.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ10565.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in regeneration of skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00037622}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KK664768; KFQ10565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PSB3; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24254:SF9; INACTIVE SERINE PROTEASE PAMR1; 1.
DR PANTHER; PTHR24254; PROTHROMBIN; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Hydrolase {ECO:0000313|EMBL:KFQ10565.1};
KW Protease {ECO:0000313|EMBL:KFQ10565.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 1..109
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 108..145
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 151..217
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 262..317
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 318..594
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 135..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 188..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ10565.1"
FT NON_TER 594
FT /evidence="ECO:0000313|EMBL:KFQ10565.1"
SQ SEQUENCE 594 AA; 66409 MW; 6CA851EACC2EA7EF CRC64;
CGQVLQASRG QILLEGYPLN ARCEWTIHVQ AGFNIELRFS MLSVEFDYMC QYDYVEVRDG
DNLDSRIIKK FCGNERPPPI RSTGSSLHVL FQSDGSKNFD GFYAVFEEIT ACSSSPCLHD
GTCILDKSGT YKCACLAGYT GNRCENFLDE KNCSDPGGPL NGYRRVVEDT GLLNGRYAKN
GTVIAFFCNN SYVLSGNEQR TCQDDGEWSG KQPICIKACR EPKISDLVRQ KVLPMQVQSR
ETPLHQLYSS AFSKQKLEIY PTKKPALPFG DLPPGYQHLH TQLQYECISP FYRRLGSSRR
TCLKTGKWSG RAPVCIPICG KAENITLQKT VTSTRWPWQA AIYRMANGVK ENSLRKGAWI
LICSGALVNE RTVVVAAHCV TDLGKTIVLK TAELKVVLGK FYRDDDRDEK TIQNLRISAI
IVHPNYDPIL LDSDIAIIKL LDKARISSRV QPICLSSSHD LTSSTEDLKI MVTGWKVLAD
IKDPGYKNDT IRMGAVRMVD SLLCEQQYED NGIQVSITDS MFCAKQDDTA FSNICPAETG
GIAAITLPGK ASPELRWHLM GLVSWGYDKT CSLQLYSGYT KALPFKDWIE KNLK
//
