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Database: UniProt
Entry: A0A2I0MS06_COLLI
LinkDB: A0A2I0MS06_COLLI
Original site: A0A2I0MS06_COLLI 
ID   A0A2I0MS06_COLLI        Unreviewed;       363 AA.
AC   A0A2I0MS06;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Protein Z, vitamin K-dependent plasma glycoprotein {ECO:0000313|EMBL:PKK32460.1};
DE   Flags: Fragment;
GN   Name=PROZ {ECO:0000313|EMBL:PKK32460.1};
GN   ORFNames=A306_00003073 {ECO:0000313|EMBL:PKK32460.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK32460.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK32460.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK32460.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:PKK32460.1}.
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DR   EMBL; AKCR02000003; PKK32460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0MS06; -.
DR   STRING; 8932.A0A2I0MS06; -.
DR   InParanoid; A0A2I0MS06; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF20; VITAMIN K-DEPENDENT PROTEIN Z; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
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};
KW   Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT   DOMAIN          55..101
FT                   /note="Gla"
FT                   /evidence="ECO:0000259|PROSITE:PS50998"
FT   DOMAIN          101..137
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          196..325
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        127..136
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PKK32460.1"
SQ   SEQUENCE   363 AA;  41211 MW;  D4C2B2F5CFFAD671 CRC64;
     TCQEGLQIPS AWSKSGSPET PQDSSAEFGL RRRALSALFI SADDANEVIK RQRRASSLLF
     EEVLPGSLER ECLEERCTHE EAREVFENDE MLKMFWDAYY GGRRCSSSPC QHNGVCEDSI
     RGYTCTCAEG YEGENCAFAK NECRHHAKEG CHHFCYPGSN SYRCSCADGY ELGKDKKQCI
     ALDQCACGRL QDSDNLIRET RKKHDERFPW QVLLLNSEGK GFCGGVLLKS NFVLTTAECA
     LLHRHFEIRI GDGPNGTSGI EKTMQVSEKH IHIRYDEDTG ENNIALLQLQ ERVECNNHQL
     PVCIPERDFA EHILIPKLAG TVSGWRMEVF REGLKRAFNT RKTIEETQQD GNHEGKHHFH
     SEE
//
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