ID G3RHH7_GORGO Unreviewed; 1101 AA.
AC G3RHH7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000015097.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000015097.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000015097.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000015097.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000015097.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; CABD030084817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030084826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3RHH7; -.
DR Ensembl; ENSGGOT00000015528.3; ENSGGOP00000015097.3; ENSGGOG00000015469.3.
DR GeneTree; ENSGT00940000158779; -.
DR HOGENOM; CLU_001634_0_2_1; -.
DR Proteomes; UP000001519; Chromosome 12.
DR Bgee; ENSGGOG00000015469; Expressed in testis and 1 other cell type or tissue.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF174; OVOSTATIN HOMOLOG 1-RELATED; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE 3: Inferred from homology;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 179..317
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 459..549
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1101 AA; 124118 MW; 6AD73E4FC7A57F19 CRC64;
RIFQWQNVTS FRNITQLSFQ LISEPMFGDY WIVVKRNSGK TVTHQFAVKR YVLPKFEVTV
NAPQTVTISD DEFQVDVCAK LRQENCFHIN YSFLVQLKFS DPSNVPMVNK LLQLELNDEF
IGNYTTDENG EAQFSIDTSD IFDPEFNLKS CYLPSWLTPQ YLDAHFLVSR FYSRTNSFLK
IVPEPKQLEC NQQKVVTVHY SLNSEAYEDD SNVKFFYLHR ISSSPIYTTW NGNFLFPISI
SADLAPAAVL FVYTLHPSGE IVADSVRFQV DKCFKHKVNI KFSNEQGLPG SNASLYLQAA
PDLFCALGAV DRNVLLLKSE QQLSAESVYN MVPSIEPYGY CYHGLNLDDG KEDPCIPQRD
MFYNGLYYTP VSNCGDGDIY NIVRNMGLKV FTNLHYRKPE VCVMERRLPL PKPLYLETEN
YGPMHSVPSR IASSGIRGEN ADCVEQAIIQ TVRTNFPETW MWDLVSVDSS GSANLLFLIP
DTVTQWEASG FCVNGDVGFG ISSTTTLEVS RPFFIEIASP FSVVQNEQFD LIVNVFSYLN
TCVEISVQVE ESQNYEANIH TWKINGSEVI QAGGRKTNIW TIIPKKLGKQ LSIYMPFSEC
TIILNWVKTP NSSPLINNFI FILGAKASKQ GVLDLPNDVV EGSAGGFFTA VGDILGLAMQ
NLVVLQMPYG SGEQNAALLA SDTYVLDYLK STEQLTEEAQ SKAFFLLSNG YQRQLSFKNS
DGSCSVFWKQ NQKGSICALT FKTLERMKKY VFIDENVQKQ TLIWLSSQQK TSGCFKNDGQ
LFNHAWEGGD EEDISLTAYV VEMFFEAGLN FTFPALRNTL FCLEVALDSG VTDGYSHAIL
AYAFALAGKE KQVESLLQTL DQSAPKLNNV IYWERERKPK TEEFPSFIPW APSAQTEKSC
YVLLAVISRK IPDLTYASKI VQWLAQWMNS HGGFSSNQVI YVGLIFIAIS RGEEGLFSKN
QNTVTFSSEG SSEIFQVNGH NRLLVQRSEV TQAPGQYTVD VEGHGCTFIQ ATLKYNVLLP
KKASGFSLSL EIVKNYSSTV FDLTVTLKYT GICNKSSMVV IDVKMLSGFT PTMSSIEEIN
NRSLIFQHKD SYIDRQFHFF C
//