ID A0A2R9A8G8_PANPA Unreviewed; 860 AA.
AC A0A2R9A8G8;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Fertilin alpha-I {ECO:0008006|Google:ProtNLM};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011701.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000011701.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000011701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AJFE02116482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9A8G8; -.
DR STRING; 9597.ENSPPAP00000011701; -.
DR Ensembl; ENSPPAT00000034362.1; ENSPPAP00000011701.1; ENSPPAG00000029052.1.
DR GeneTree; ENSGT00940000161891; -.
DR Proteomes; UP000240080; Chromosome 12.
DR Bgee; ENSPPAG00000029052; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF120; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 1A-RELATED; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 224..418
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 427..511
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 652..686
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 762..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 483..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 676..685
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 860 AA; 95060 MW; 6CD45578F85CC312 CRC64;
MSLVALLKDS AKIKFQTWAP QKWNLRLGLV PGPSCIRLEI LMLLVIFVPS MYCHLGSIYY
SFYEIIIPKR LTVQGGDIPV EGLSYLLLMQ GQKHLVHLKV KRNHFVNNFP VYSYHNGLLG
QESPFISHDC HYEGYIEGVS GSFVSVNICA GLRGILIKEE KSYSSEPMDS SRRFEHVLYT
MAHQARVSCG VTSRDSHVVS TSWQQGSRKP HDLQALSYLW SHKKYVEMFV VVNNQRFQMW
GSNVNETVQT VVDVIALANS FTRGINTEVV LAGMEIWTEG DLIDVTVDLQ ITLRNFNHWR
QEMLFHRAKH DVAHMIVGHH PGQNMGQAFL SGACSSGFVA AVESFHHEDA LLFAALMAHE
LGHNLGIQHD HSACFCKDKH FCLMHENITK ESGFSNCSSD YYYQFLREHK GACLFNKPWP
RGRKRRDSAC GNGVVEDTEQ CDCGSACHLD PCCDATCTLK ENVECSHGLC CLGCTFRRKG
FLCHPTQDEC DLPEYCDGSS AECPADSYKQ DGTLYDRIHY CSGGQCKNPD NQCVNIYGYP
ARSAPEDCYI SINTRGDRFG NCGRPTEDQQ TYVICSGDNV FCGKLICTGV QSLPRVKAQH
TVIQVPHDND WCWSMDAHNI TDIPDDGDVR VGTSCAPNKV CMDHSCVHHS ILLYDCRTEE
SCHGKGVCNN LRHCHCEFGF APPDCKNPGN GGSVDSGPPG MQVTNNNESG IEGSARVQRQ
RQDLDYKLIV FLVPLFLVLL LCTPLTMSYL CSEVQTAVAE VEESSTETTL ESELTSADKI
PTAEEILPPD EEAPPPGEEA PPPAEAPPPA EAPPPEAAPP PEAAPPPQAP PPEAPPTPQA
PRPEASPAPQ APPPEAPPAQ
//
