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Database: UniProt
Entry: A0A2K6BRX3_MACNE
LinkDB: A0A2K6BRX3_MACNE
Original site: A0A2K6BRX3_MACNE 
ID   A0A2K6BRX3_MACNE        Unreviewed;       472 AA.
AC   A0A2K6BRX3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Serpin family A member 10 {ECO:0000313|Ensembl:ENSMNEP00000014117.1};
GN   Name=SERPINA10 {ECO:0000313|Ensembl:ENSMNEP00000014117.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000014117.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000014117.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   AlphaFoldDB; A0A2K6BRX3; -.
DR   STRING; 9545.ENSMNEP00000014117; -.
DR   Ensembl; ENSMNET00000038320.1; ENSMNEP00000014117.1; ENSMNEG00000031236.1.
DR   GeneTree; ENSGT00940000159462; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000031236; Expressed in liver and 12 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   CDD; cd02055; serpinA10_PZI; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   InterPro; IPR033835; PZI_serpin_dom.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461:SF191; PROTEIN Z-DEPENDENT PROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00780; LEUSERPINII.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT   DOMAIN          112..469
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          53..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53203 MW;  DDA6BB1049C10BD2 CRC64;
     LLEQEGKTQH LEAVTSAEGR HSLASAADHM KVVPSLLLSV LLAQVWLVPS LAPSPQSPEA
     PALQNQTGGV VQAPREEEED EEEASEKAGE EEKAWLIASG QQLAKETSNF GFSLLRKISM
     RHDGNMVFSP FGVSLAMAGL MLGATGPTKA QIKTGLHLQS LNTTKPGLLP SLFKGLRETL
     SHNLELGLTQ GSFAFIHKDF DVKELFLNLS KRYFDTECVL MNFHNASQAK RLMNHYINKE
     TQGKIPKLFD EIYPETKLIL VDYILFKGKW LTPFDPVFTE ADTFHLDKYK TIKVSMMYGA
     GKFASTFDKN FHCHVLKLPY QGNATMLVVL MEKMGDHLAL EDYLTTDLVE TWLRNMKTRN
     MEVFFPKFKL DQKYEMHELL KQMGIRRIFS PWADLSELSA TGRNLQVSRV LQRTVIEVDE
     RGTEAVAGTL SEIIAYSMPP VIKVNRPFHF MIYEETSGML LFLGRVVNPT LL
//
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