ID A0A091I8S3_CALAN Unreviewed; 695 AA.
AC A0A091I8S3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=N300_01952 {ECO:0000313|EMBL:KFO96155.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO96155.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO96155.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO96155.1};
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; KL217512; KFO96155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091I8S3; -.
DR STRING; 9244.A0A091I8S3; -.
DR Proteomes; UP000054308; 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; 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 SMART; SM00032; CCP; 2.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 2.
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:KFO96155.1};
KW Protease {ECO:0000313|EMBL:KFO96155.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 104..212
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 211..248
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 254..320
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 365..420
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 421..695
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 238..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 291..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO96155.1"
FT NON_TER 695
FT /evidence="ECO:0000313|EMBL:KFO96155.1"
SQ SEQUENCE 695 AA; 77939 MW; B988E367047F5ED0 CRC64;
EYTVINENCP GAEWNIMCRE CCEYDQIECI CPGQKERVGY TIPCCRNEDN ECDSCLIHPG
CTIFENCKSC RNGSWGGKLD NFYIKGIYCA ECRAGWYGGD CMRCGQVFRV SRGQILLEGY
PLNARCEWTI HVPAGFNIEL RFSMLSLEFD YMCQYDYVEV RDGDNLDSQI IKRFCGNERP
PPIRSTGSSL HVLFQSDGSK NFDGFHAVFE ETTACSSFPC HHDGTCILDK SGTYRCACLA
GYTGKHCENF LDEKNCSDPG GPLNGYRRVV EDTGLLNGHY AKIGTVIAFF CNNSYVLSGN
EQRTCQDNGE WSGNQPICIK ACREPKISDL VRQKVLPMQV QSRETPLHQL YSSAFSKQKL
EIYPTKKPAL PFGDLPAGYQ HLHTQLQYEC ISPFYRRLGS SRRTCLKTGK WSGRAPVCIP
ICGKAENITL QKTSIRWPWQ AAIYRMVNGM KEKSLQKGTW ILICSGALVN ERTVVAAAHC
VTDLGKTTVL NTAELKVVLG KFYRDDDRDE KTIQNLQISA IIVHPNYDPI LLDSDIAIIK
LLDKARISSH VQPICLSSAH DLTTSTEDLK IMVTGWKVLA DIKDPGYKND TIRMGAVQMV
DSLLCEQQYD DNGIQVSITD SMFCAKQDHT AFSNICPAET GGIAAITLLG KASPELRWHL
VGLVSWGYDK TCSTGLYSGY TKAFLFKDWI EKNLK
//
