ID A0A7J8E0X9_MOLMO Unreviewed; 1037 AA.
AC A0A7J8E0X9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 14.
DE SubName: Full=Cysteine rich transmembrane BMP regulator 1 {ECO:0000313|EMBL:KAF6429157.1};
GN ORFNames=HJG59_003343 {ECO:0000313|EMBL:KAF6429157.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6429157.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6429157.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6429157.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6429157.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:KAF6429157.1}.
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DR EMBL; JACASF010000015; KAF6429157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8E0X9; -.
DR FunCoup; A0A7J8E0X9; 530.
DR InParanoid; A0A7J8E0X9; -.
DR OrthoDB; 5976811at2759; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR FunFam; 2.10.22.10:FF:000002; Cysteine rich transmembrane BMP regulator 1; 1.
DR FunFam; 4.10.40.20:FF:000003; cysteine-rich motor neuron 1 protein isoform X1; 1.
DR FunFam; 2.10.22.10:FF:000004; cysteine-rich motor neuron 1 protein isoform X2; 1.
DR Gene3D; 4.10.40.20; -; 1.
DR Gene3D; 6.20.200.20; -; 5.
DR Gene3D; 2.10.22.10; Antistasin, domain 1; 4.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR052624; CRIM1.
DR InterPro; IPR045813; CRIM1_C.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011061; Hirudin/antistatin.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46439; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
DR PANTHER; PTHR46439:SF1; CYSTEINE-RICH MOTOR NEURON 1 PROTEIN; 1.
DR Pfam; PF02822; Antistasin; 4.
DR Pfam; PF19442; CRIM1_C; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF00093; VWC; 6.
DR SMART; SM00121; IB; 1.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 3.
DR SUPFAM; SSF57603; FnI-like domain; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57262; Leech antihemostatic proteins; 3.
DR PROSITE; PS51252; ANTISTASIN; 4.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:KAF6429157.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1037
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029488803"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..112
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 334..391
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 401..457
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 469..498
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 505..532
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 539..564
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 567..592
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 606..663
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 677..735
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 751..809
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT DOMAIN 817..874
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
SQ SEQUENCE 1037 AA; 113832 MW; B8E3B8C28AAD3C74 CRC64;
MYLVAGGRGL AGCGHLLVSL LGLLLLLARS GTRALVCLPC DESKCEEPRN CPGSIVQGVC
GCCYMCARQR NESCGGAYGL HGACDRGLRC VIRPPLNGDS ITEYEVGVCE DENWDDDQLL
GFEPCKENLV SGCNIINGKC ECVTIRTCNN PFEFPRKDMC LSALKRIQEE KPDCSKARCE
VQFSPRCPED SVLIEGYAPP GKCCPLPSRC VCDPAGCLRK VCQPGYLNIL VSKASGKPGE
CCDLYECKPV FSVDCSTVEC PSVQQAVCPL DSYETQVRLT ADGCCTLPTR CECLSGLCGF
PVCEVGSIPR IVSRGDGTPG KCCDVFECVN ETKPACMFNN VEYNDGDMFR LDKCRFCRCQ
GGVAICFTAQ CGELNCERYY VPEGECCPVC EDPVYPFNNP AGCYANGQIR AHGDRWREDD
CTFCQCINGE SHCVATVCGQ SCMNPVKVPG ECCPVCEEPT YITIDPPACG ELSNCTLTEK
DCIYGFKLDH SGCRTCQCKS REELCTGLRR GCTLDCPFGF LTDAHGCEIC RCRPRPKKCR
PIICDKYCPF GYLKNKHGCD ICRCRKCPEL PCGKTCPLGF QKDSHGCSTC KCREVPTSAK
SPELSGTCLS MDGHHHRHEE SWHDGCRECY CHNGREMCAL ITCPVPACGS PTIRPGQCCP
SCSDDLVVQK PELSTPSICH APGGEYFVEG ETWNIDSCTQ CTCHSGRVMC ETEVCPPLLC
QNPSRTQDSC CPQCSDAPLQ PSAPHNDSAP SYCKNDEGDI FLAAESWKPD VCTSCVCVNS
VISCYSESCP SVSCERPVLR KGQCCPYCIE DSIARKVVCR FGGKAYADEE RWDIDSCTHC
YCLQGQTLCS TVSCPPLPCA EPLNVEGSCC PMCPEMYVPE PTNVPIEKIN HRGETDLEVP
MWPTPSENDI VHLPRDMGHL QVDHGDNNRR RPGEDPSLDS IASVVVPIVI GLSIIIAFLL
INQKKQWVPL LCWYRTPTKP SSLNNQLVSV DCKKGTRVQG DSAQRMLRIA EPDARFSGFY
SMQKQNHLQA DNFYQTV
//
