MAB7_CAEEL
ID MAB7_CAEEL Reviewed; 287 AA.
AC Q95Q39; Q3L453;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein male abnormal 7;
GN Name=mab-7 {ECO:0000312|WormBase:ZC13.4}; ORFNames=ZC13.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW59416.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND MUTAGENESIS OF CYS-67 AND
RP CYS-108.
RX PubMed=17959165; DOI=10.1016/j.ydbio.2007.09.037;
RA Tsang S.W., Nguyen C.Q., Hall D.H., Chow K.L.;
RT "mab-7 encodes a novel transmembrane protein that orchestrates sensory ray
RT morphogenesis in C. elegans.";
RL Dev. Biol. 312:353-366(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Plays an important role in determining body shape and sensory
CC ray morphology, possibly by acting as a signaling molecule outside the
CC expressing cell. {ECO:0000269|PubMed:17959165}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17959165};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:17959165}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis first at the two-fold stage
CC and throughout the larval stages but not at the adult stage. Detected
CC in the body seams after the L4 stage with expression maintained in
CC adults. Detected in the male tail structural cells at the late L4 stage
CC and also maintained in adults. Detected at different developmental
CC stages in vulva, PQR neurons and several neuronal processes in the head
CC region. {ECO:0000269|PubMed:17959165}.
CC -!- DOMAIN: The EGF-like domain and the SXC (ShKT) domain are essential for
CC the biological activity of the protein. May function as protein
CC interaction domains. {ECO:0000269|PubMed:17959165}.
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DR EMBL; AY742796; AAW59416.1; -; mRNA.
DR EMBL; FO081302; CCD70627.1; -; Genomic_DNA.
DR RefSeq; NP_508174.2; NM_075773.4.
DR AlphaFoldDB; Q95Q39; -.
DR SMR; Q95Q39; -.
DR STRING; 6239.ZC13.4; -.
DR EPD; Q95Q39; -.
DR PaxDb; Q95Q39; -.
DR PeptideAtlas; Q95Q39; -.
DR EnsemblMetazoa; ZC13.4.1; ZC13.4.1; WBGene00003104.
DR GeneID; 180440; -.
DR KEGG; cel:CELE_ZC13.4; -.
DR UCSC; ZC13.4; c. elegans.
DR CTD; 180440; -.
DR WormBase; ZC13.4; CE41485; WBGene00003104; mab-7.
DR eggNOG; KOG3371; Eukaryota.
DR GeneTree; ENSGT00970000196680; -.
DR HOGENOM; CLU_1035278_0_0_1; -.
DR InParanoid; Q95Q39; -.
DR OMA; RWALEDK; -.
DR OrthoDB; 986766at2759; -.
DR PhylomeDB; Q95Q39; -.
DR PRO; PR:Q95Q39; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003104; Expressed in embryo and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd07828; lipocalin_heme-bd-THAP4-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR045165; Nitrobindin.
DR InterPro; IPR003582; ShKT_dom.
DR InterPro; IPR014878; THAP4-like_heme-bd.
DR PANTHER; PTHR15854; PTHR15854; 1.
DR SMART; SM00181; EGF; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..287
FT /note="Protein male abnormal 7"
FT /id="PRO_0000409248"
FT TRANSMEM 1..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000269|PubMed:17959165"
FT TOPO_DOM 23..287
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 34..68
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 71..108
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..49
FT /evidence="ECO:0000255"
FT DISULFID 43..56
FT /evidence="ECO:0000255"
FT DISULFID 58..67
FT /evidence="ECO:0000255"
FT MUTAGEN 67
FT /note="C->Y: In allele e1599; hermaphrodites and adult
FT males appear slightly dumpy, with males having swollen
FT bursal rays and much lower mating efficiency than that of
FT wild-type males. When subjected to RNAi knock-down of mab-7
FT gene, no obvious enhancement of severity in phenotype was
FT observed."
FT /evidence="ECO:0000269|PubMed:17959165"
FT MUTAGEN 108
FT /note="C->Y: In allele wx74; hermaphrodites and adult males
FT appear slightly dumpy, with males having swollen bursal
FT rays and much lower mating efficiency than that of wild-
FT type males. When subjected to RNAi knock-down of mab-7
FT gene, no obvious enhancement of severity in phenotype was
FT observed."
FT /evidence="ECO:0000269|PubMed:17959165"
SQ SEQUENCE 287 AA; 32344 MW; CEF52C1C6A3C8F16 CRC64;
MTITRILTCL LICLFIRIPA AGTKTTQLIF KRFTEETCQN DPCLNGGTCT PGKLSCTCAT
GWMGRYCHRK CRNIYKSCDR WAVEDKCHTI LTQTNFFDVN CAISCKMCSP DPNYVAPEIP
LAPALEPMQF FLGKWHSRAS KGLRFPTDLY DTEYEEIIDI APANVPMFGP PSLNFTSTSW
FGDDTRVVHG FITLKPNSFP PEVAILSTSN EGLNMIELGT LKHHVLTLNV SYMQVHPTMD
SKVLPLGATR RLRRVGSLLE MTVAKLFSEN KVSQFKKMFK KIADYAF
