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Database: UniProt
Entry: G3VJU8_SARHA
LinkDB: G3VJU8_SARHA
Original site: G3VJU8_SARHA 
ID   G3VJU8_SARHA            Unreviewed;       579 AA.
AC   G3VJU8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN   Name=FKBP10 {ECO:0000313|Ensembl:ENSSHAP00000003453.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000003453.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000003453.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000003453.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
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DR   AlphaFoldDB; G3VJU8; -.
DR   STRING; 9305.ENSSHAP00000003453; -.
DR   Ensembl; ENSSHAT00000003489.2; ENSSHAP00000003453.2; ENSSHAG00000003034.2.
DR   eggNOG; KOG0549; Eukaryota.
DR   GeneTree; ENSGT00940000156331; -.
DR   HOGENOM; CLU_041087_0_0_1; -.
DR   InParanoid; G3VJU8; -.
DR   TreeFam; TF105296; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005528; F:FK506 binding; IEA:Ensembl.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.10.50.40; -; 4.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR46046:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP10; 1.
DR   PANTHER; PTHR46046; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF00254; FKBP_C; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF54534; FKBP-like; 4.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50059; FKBP_PPIASE; 4.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..579
FT                   /note="peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5029560340"
FT   DOMAIN          59..147
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          171..259
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          283..371
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          396..483
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          501..529
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          539..574
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          533..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   579 AA;  63838 MW;  78B9B035B4851400 CRC64;
     MSPWGSLSRI LPLFPALLLL LQASGRALGR ASPGGGPLED VVIERYHVPR GCPREVQMGD
     FIRYHYNGTF EDGKKFDSSY DRGVTVAGVV GVGRLITGMD RGLMGMCVNE RRRLIVPPHL
     GYGSIGVAGL IPPDSTLYFD VVLLDVWNKE DSVQVNTLLR PTNCPRMVQD SDFVRYHYNG
     TLLDGTAFDS SYSRSSTYDT YVGSGWLIKG MDQGLLGMCP GEKRKIIIPP FLAYGEKGYG
     TVIPPQASLV FHVLLIDVHN PKDSVQLETL LLPPGCGRKA VAGDFMRYHY NGSLMDGTIF
     DSSYSRNHTY NTYIGQGYII PGMDQGLQGV CIGELRRITI PPHLAYGENG AGDKIPGSAV
     LIFDVHVIDF HNPSDPVETR TISRPSEGCN ETSKLGDFVR YHYNCSLLDG TKLFSSHDYG
     EPQEATLGAN KVIEGLNTGL QGMCVGERRQ LIIPPHLGHG ENGARGVPGS AVLLFEVELV
     SREEGLPEGY LFVWHGDPPP NLYEDMDLNK DGEIPLEEFS TFIKAQVAEG KGKLIPGQDP
     EKTIGDMFQN QDRNQDGKIT MEELKLKSDE DRERVHEEL
//
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